Nucleic acid and amino acid sequences relating to Streptococcus pneumoniae for diagnostics and therapeutics

ABSTRACT

The invention provides isolated polypeptide and nucleic acid sequences derived from  Streptococcus pneumoniae  that are useful in diagnosis and therapy of pathological conditions; antibodies against the polypeptides; and methods for the production of the polypeptides. The invention also provides methods for the detection, prevention and treatment of pathological conditions resulting from bacterial infection.

RELATED APPLICATIONS

This application is a continuation of U.S. application Ser. No.11/027,892 (now U.S. Pat. No. 7,378,514), filed Dec. 30, 2004, which isa continuation of U.S. application Ser. No. 10/640,833 (now abandoned),filed Aug. 14, 2003, which is a continuation of U.S. application Ser.No. 09/583,110 (now U.S. Pat. No. 6,699,703) filed May 26, 2000, whichis a continuation-in-part of U.S. application Ser. No. 09/107,433 (nowU.S. Pat. No. 6,800,744), filed Jun. 30, 1998, which claims the benefitof U.S. Application No. 60/085,131, filed May 12, 1998 and of U.S.Application No. 60/051,553, filed Jul. 2, 1997. The entire teachings ofthe above applications are incorporated herein by reference.

INCORPORATION BY REFERENCE OF MATERIAL ON COMPACT DISK

This application incorporates by reference the Sequence Listingcontained on the two compact disks (Copy 1 and Copy 2), filedconcurrently herewith, containing the following file:

File name: 3687.1000-041SequenceList.txt; created Sep. 16, 2006, 8,135KB in size.

This application also incorporates by reference Table 2 contained on thetwo compact disks (Copy 1 and Copy 2), filed concurrently herewith,containing the following file:

File name: Table2_(—)2.txt; created Aug. 21, 2006, 351 KB in size.

TABLES The patent contains table(s) that have been included at the endof the specification.

FIELD OF THE INVENTION

The invention relates to isolated nucleic acids and polypeptides derivedfrom Streptococcus pneumoniae that are useful as molecular targets fordiagnostics, prophylaxis and treatment of pathological conditions, aswell as materials and methods for the diagnosis, prevention, andamelioration of pathological conditions resulting from bacterialinfection.

BACKGROUND OF THE INVENTION

Streptococcus pneumoniae (S. pneumoniae) is a common, spherical,gram-positive bacterium. Worldwide it is a leading cause of illnessamong children, the elderly, and individuals with debilitating medicalconditions (Breiman, R. F. et al., 1994, JAMA 271: 1831). S. pneumoniaeis estimated to be the causal agent in 3,000 cases of meningitis, 50,000cases of bacteremia, 500,000 cases of pneumonia, and 7,000,000 cases ofotitis media annually in the United States alone (Reichler, M. R. etal., 1992, J. Infect. Dis. 166: 1346; Stool, S. E. and Field, M. J.,1989 Pediatr. Infect. Dis J. 8: S11). In the United States alone, 40,000deaths result annually from S. pneumoniae infections (Williams, W. W. etal., 1988 Ann. Intern. Med. 108: 616) with a death rate approaching 30%from bacteremia (Butler, J. C. et al., 1993, JAMA 270: 1826).Pneumococcal pneumonia is a serious problem among the elderly ofindustrialized nations (Käyhty, H. and Eskola, J., 1996 Emerg. Infect.Dis. 2: 289) and is a leading cause of death among children indeveloping nations (Käyhty, H. and Eskola, J., 1996 Emerg. Infect. Dis.2: 289; Stansfield, S. K., 1987 Pediatr. Infect. Dis. 6: 622).

Vaccines against S. pneumoniae have been available for a number ofyears. There are a large number of serotypes based on the polysaccharidecapsule (van Dam, J. E., Fleer, A., and Snippe, H., 1990 Antonie vanLeeuwenhoek 58: 1) although only a fraction of the serotypes seem to beassociated with infections (Martin, D. R. and Brett, M. S., 1996 N. Z.Med. J. 109: 288). A multivalent vaccine against capsularpolysaccharides of 23 serotypes (Smart, L. E., Dougall, A. J. andGridwood, R. W., 1987 J. Infect. 14: 209) has provided protection forsome groups but not for several groups at risk for pneumococcalinfections, such as infants and the elderly (Mäkel, P. H. et al., 1980Lancet 2: 547; Sankilampi, U., 1996 J. Infect. Dis. 173: 387).Conjugated pneumococcal capsular polysaccharide vaccines have somewhatimproved efficacy, but are costly and, therefore, are not likely to bein widespread use (Käyhty, H. and Eskola, J., 1996 Emerg. Infect. Dis.2: 289).

At one time, S. pneumoniae strains were uniformly susceptible topenicillin. The report of a penicillin-resistant strain of (Hansman, D.and Bullen, M. M., 1967 Lancet 1: 264) was followed rapidly by manyreports indicating the worldwide emergence of penicillin-resistant andpenicillin non-susceptible strains (Klugman, K. P., 1990 Clin.Microbiol. Rev. 3: 171). S. pneumoniae strains which are resistant tomultiple antibiotics (including penicillin) have also been observedrecently within the United States (Welby, P. L., 1994 Pediatr. Infect.Dis. J. 13: 281; Ducin, J. S. et al., 1995 Pediatr. Infect. Dis. J. 14:745; Butler, J. C., 1996 J. Infect. Dis. 174: 986) as well asinternationally (Boswell, T. C. et al., 1996; J. Infect. 33: 17;Catchpole, C., Fraise, A., and Wise, R., 1996 Microb. Drug Resist. 2:431; Tarasi, A. et al., 1997 Microb. Drug Resist. 3: 105).

A high incidence of morbidity is associated with invasive S. pneumoniaeinfections (Williams, W. W. et al., 1988 Ann. Intern. Med. 108: 616).Because of the incomplete effectiveness of currently available vaccinesand antibiotics, the identification of new targets for antimicrobialtherapies, including, but not limited to, the design of vaccines andantibiotics, which may help prevent infection or that may be useful infighting existing infections, is highly desirable.

SUMMARY OF THE INVENTION

The present invention fulfills the need for diagnostic tools andtherapeutics by providing bacterial-specific compositions and methodsfor detecting, treating, and preventing bacterial infection, inparticular S. pneumoniae infection.

The present invention encompasses isolated polypeptides and nucleicacids derived from S. pneumoniae that are useful as reagents fordiagnosis of bacterial infection, components of effective antibacterialvaccines, and/or as targets for antibacterial drugs, including anti-S.pneumoniae drugs. The nucleic acids and peptides of the presentinvention also have utility for diagnostics and therapeutics for S.pneumoniae and other Streptococcus species. They can also be used todetect the presence of S. pneumoniae and other Streptococcus species ina sample; and in screening compounds for the ability to interfere withthe S. pneumoniae life cycle or to inhibit S. pneumoniae infection. Morespecifically, this invention features compositions of nucleic acidscorresponding to entire coding sequences of S. pneumoniae proteins,including surface or secreted proteins or parts thereof, nucleic acidscapable of binding mRNA from S. pneumoniae proteins to block proteintranslation, and methods for producing S. pneumoniae proteins or partsthereof using peptide synthesis and recombinant DNA techniques. Thisinvention also features antibodies and nucleic acids useful as probes todetect S. pneumoniae infection. In addition, vaccine compositions andmethods for the protection or treatment of infection by S. pneumoniaeare within the scope of this invention.

The nucleotide sequences provided in SEQ ID NO: 1-SEQ ID NO: 2661, afragment thereof, or a nucleotide sequence at least 99.5% identical to asequence contained within SEQ ID NO: 1-SEQ ID NO: 2661 may be “provided”in a variety of medias to facilitate use thereof. As used herein,“provided” refers to a manufacture, other than an isolated nucleic acidmolecule, which contains a nucleotide sequence of the present invention,i.e., the nucleotide sequence provided in SEQ ID NO: 1-SEQ ID NO: 2661,a fragment thereof, or a nucleotide sequence at least 99.5% identical toa sequence contained within SEQ ID NO: 1-SEQ ID NO: 2661. Uses for andmethods for providing nucleotide sequences in a variety of media is wellknown in the art (see e.g., EPO Publication No. EP 0 756 006)

In one application of this embodiment, a nucleotide sequence of thepresent invention can be recorded on computer readable media. As usedherein, “computer readable media” refers to any media which can be readand accessed directly by a computer. Such media include, but are notlimited to: magnetic storage media, such as floppy discs, hard discstorage media, and magnetic tape; optical storage media such as CD-ROM;electrical storage media such as RAM and ROM; and hybrids of thesecategories such as magnetic/optical storage media. A person skilled inthe art can readily appreciate how any of the presently known computerreadable media can be used to create a manufacture comprising computerreadable media having recorded thereon a nucleotide sequence of thepresent invention.

As used herein, “recorded” refers to a process for storing informationon computer readable media. A person skilled in the art can readilyadopt any of the presently known methods for recording information oncomputer readable media to generate manufactures comprising thenucleotide sequence information of the present invention.

A variety of data storage structures are available to a person skilledin the art for creating a computer readable media having recordedthereon a nucleotide sequence of the present invention. The choice ofthe data storage structure will generally be based on the means chosento access the stored information. In addition, a variety of dataprocessor programs and formats can be used to store the nucleotidesequence information of the present invention on computer readablemedia. The sequence information can be represented in a word processingtext file, formatted in commercially-available software such asWordPerfect and Microsoft Word, or represented in the form of an ASCIIfile, stored in a database application, such as DB2, Sybase, Oracle, orthe like. A person skilled in the art can readily adapt any number ofdata processor structuring formats (e.g. text file or database) in orderto obtain computer readable media having recorded thereon the nucleotidesequence information of the present invention.

By providing the nucleotide sequence of SEQ ID NO: 1-SEQ ID NO: 2661, afragment thereof, or a nucleotide sequence at least 99.5% identical to asequence contained within SEQ ID NO: 1-SEQ ID NO: 2661 in computerreadable form, a person skilled in the art can routinely access thesequence information for a variety of purposes. Computer software ispublicly available which allows a person skilled in the art to accesssequence information provided in a computer readable media. Examples ofsuch computer software include programs of the “Staden Package”, “DNAStar”, “MacVector”, GCG “Wisconsin Package” (Genetics Computer Group,Madison, Wis.) and “NCBI toolbox” (National Center for BiotechnologyInformation).

Computer algorithms enable the identification of S. pneumoniae openreading frames (ORFs) within SEQ ID NO: 1-SEQ ID NO: 2661 which containhomology to ORFs or proteins from other organisms. Examples of suchsimilarity-search algorithms include the BLAST [Altschul et al., J. Mol.Biol. 215:403-410 (1990)] and Smith-Waterman [Smith and Waterman (1981)Advances in Applied Mathematics, 2:482-489] search algorithms. Thesealgorithms are utilized on computer systems as exemplified below. TheORFs so identified represent protein encoding fragments within the S.pneumoniae genome and are useful in producing commercially importantproteins such as enzymes used in fermentation reactions and in theproduction of commercially useful metabolites.

The present invention further provides systems, particularlycomputer-based systems, which contain the sequence information describedherein. Such systems are designed to identify commercially importantfragments of the S. pneumoniae genome. As used herein, “a computer-basedsystem” refers to the hardware means, software means, and data storagemeans used to analyze the nucleotide sequence information of the presentinvention. The minimum hardware means of the computer-based systems ofthe present invention comprises a central processing unit (CPU), inputmeans, output means, and data storage means. A person skilled in the artcan readily appreciate that any one of the currently availablecomputer-based systems is suitable for use in the present invention. Thecomputer-based systems of the present invention comprise a data storagemeans having stored therein a nucleotide sequence of the presentinvention and the necessary hardware means and software means forsupporting and implementing a search means. As used herein, “datastorage means” refers to memory which can store nucleotide sequenceinformation of the present invention, or a memory access means which canaccess manufactures having recorded thereon the nucleotide sequenceinformation of the present invention.

As used herein, “search means” refers to one or more programs which areimplemented on the computer-based system to compare a target sequence ortarget structural motif with the sequence information stored within thedata storage means. Search means are used to identify fragments orregions of the S. pneumoniae genome which are similar to, or “match”, aparticular target sequence or target motif. A variety of knownalgorithms are known in the art and have been disclosed publicly, and avariety of commercially available software for conducting homology-basedsimilarity searches are available and can be used in the computer-basedsystems of the present invention. Examples of such software include, butis not limited to, FASTA (GCG Wisconsin Package), Bic_SW (CompugenBioccelerator, BLASTN2, BLASTP2 and BLASTX2 (NCBI) and Motifs (GCG).BLASTN2, A person skilled in the art can readily recognize that any oneof the available algorithms or implementing software packages forconducting homology searches can be adapted for use in the presentcomputer-based systems.

As used herein, a “target sequence” can be any DNA or amino acidsequence of six or more nucleotides or two or more amino acids. A personskilled in the art can readily recognize that the longer a targetsequence is, the less likely a target sequence will be present as arandom occurrence in the database. The most preferred sequence length ofa target sequence is from about 10 to 100 amino acids or from about 30to 300 nucleotide residues. However, it is well recognized that manygenes are longer than 500 amino acids, or 1.5 kb in length, and thatcommercially important fragments of the S. pneumoniae genome, such assequence fragments involved in gene expression and protein processing,will often be shorter than 30 nucleotides.

As used herein, “a target structural motif,” or “target motif,” refersto any rationally selected sequence or combination of sequences in whichthe sequence(s) are chosen based on a specific functional domain orthree-dimensional configuration which is formed upon the folding of thetarget polypeptide. There are a variety of target motifs known in theart. Protein target motifs include, but are not limited to, enzymaticactive sites, membrane spanning regions, and signal sequences. Nucleicacid target motifs include, but are not limited to, promoter sequences,hairpin structures and inducible expression elements (protein bindingsequences).

A variety of structural formats for the input and output means can beused to input and output the information in the computer-based systemsof the present invention. A preferred format for an output means ranksfragments of the S. pneumoniae genome possessing varying degrees ofhomology to the target sequence or target motif. Such presentationprovides a person skilled in the art with a ranking of sequences whichcontain various amounts of the target sequence or target motif andidentifies the degree of homology contained in the identified fragment.

A variety of comparing means can be used to compare a target sequence ortarget motif with the data storage means to identify sequence fragmentsof the S. pneumoniae genome. In the present examples, implementingsoftware which implement the BLASTP2 and bic_SW algorithms (Altschul etal., J. Mol. Biol. 215:403-410 (1990); Compugen Biocellerator) was usedto identify open reading frames within the S. pneumoniae genome. Aperson skilled in the art can readily recognize that any one of thepublicly available homology search programs can be used as the searchmeans for the computer-based systems of the present invention.

The invention features S. pneumoniae polypeptides, preferably asubstantially pure preparation of an S. pneumoniae polypeptide, or arecombinant S. pneumoniae polypeptide. In preferred embodiments: thepolypeptide has biological activity; the polypeptide has an amino acidsequence at least 60%, 70%, 80%, 90%, 95%, 98%, or 99% identical to anamino acid sequence of the invention contained in the Sequence Listing,preferably it has about 65% sequence identity with an amino acidsequence of the invention contained in the Sequence Listing, and mostpreferably it has about 92% to about 99% sequence identity with an aminoacid sequence of the invention contained in the Sequence Listing; thepolypeptide has an amino acid sequence essentially the same as an aminoacid sequence of the invention contained in the Sequence Listing; thepolypeptide is at least 5, 10, 20, 50, 100, or 150 amino acid residuesin length; the polypeptide includes at least 5, preferably at least 10,more preferably at least 20, more preferably at least 50, 100, or 150contiguous amino acid residues of the invention contained in theSequence Listing. In yet another preferred embodiment, the amino acidsequence which differs in sequence identity by about 7% to about 8% fromthe S. pneumoniae amino acid sequences of the invention contained in theSequence Listing is also encompassed by the invention.

In preferred embodiments: the S. pneumoniae polypeptide is encoded by anucleic acid of the invention contained in the Sequence Listing, or by anucleic acid having at least 60%, 70%, 80%, 90%, 95%, 98%, or 99%homology with a nucleic acid of the invention contained in the SequenceListing.

In a preferred embodiment, the subject S. pneumoniae polypeptide differsin amino acid sequence at 1, 2, 3, 5, 10 or more residues from asequence of the invention contained in the Sequence Listing. Thedifferences, however, are such that the S. pneumoniae polypeptideexhibits an S. pneumoniae biological activity, e.g., the S. pneumoniaepolypeptide retains a biological activity of a naturally occurring S.pneumoniae enzyme.

In preferred embodiments, the polypeptide includes all or a fragment ofan amino acid sequence of the invention contained in the SequenceListing; fused, in reading frame, to additional amino acid residues,preferably to residues encoded by genomic DNA 5′ or 3′ to the genomicDNA which encodes a sequence of the invention contained in the SequenceListing.

In yet other preferred embodiments, the S. pneumoniae polypeptide is arecombinant fusion protein having a first S. pneumoniae polypeptideportion and a second polypeptide portion, e.g., a second polypeptideportion having an amino acid sequence unrelated to S. pneumoniae. Thesecond polypeptide portion can be, e.g., any ofglutathione-5-transferase, a DNA binding domain, or a polymeraseactivating domain. In preferred embodiment the fusion protein can beused in a two-hybrid assay.

Polypeptides of the invention include those which arise as a result ofalternative transcription events, alternative RNA splicing events, andalternative translational and postranslational events.

In a preferred embodiment, the encoded S. pneumoniae polypeptide differs(e.g., by amino acid substitution, addition or deletion of at least oneamino acid residue) in amino acid sequence at 1, 2, 3, 5, 10 or moreresidues, from a sequence of the invention contained in the SequenceListing. The differences, however, are such that: the S. pneumoniaeencoded polypeptide exhibits a S. pneumoniae biological activity, e.g.,the encoded S. pneumoniae enzyme retains a biological activity of anaturally occurring S. pneumoniae.

In preferred embodiments, the encoded polypeptide includes all or afragment of an amino acid sequence of the invention contained in theSequence Listing; fused, in reading frame, to additional amino acidresidues, preferably to residues encoded by genomic DNA 5′ or 3′ to thegenomic DNA which encodes a sequence of the invention contained in theSequence Listing.

The S. pneumoniae strain, 14453, from which genomic sequences have beensequenced, has been deposited on Jun. 26, 1997 in the American TypeCulture Collection, 10801 University Blvd., Manassas, Va. 20110-2209,and assigned the ATCC designation # 55987.

Included in the invention are: allelic variations; natural mutants;induced mutants; proteins encoded by DNA that hybridize under high orlow stringency conditions to a nucleic acid which encodes a polypeptideof the invention contained in the Sequence Listing (for definitions ofhigh and low stringency see Current Protocols in Molecular Biology, JohnWiley & Sons, New York, 1989, 6.3.1-6.3.6, hereby incorporated byreference); and, polypeptides specifically bound by antisera to S.pneumoniae polypeptides, especially by antisera to an active site orbinding domain of S. pneumoniae polypeptide. The invention also includesfragments, preferably biologically active fragments. These and otherpolypeptides are also referred to herein as S. pneumoniae polypeptideanalogs or variants.

The invention further provides nucleic acids, e.g., RNA or DNA, encodinga polypeptide of the invention. This includes double stranded nucleicacids as well as coding and antisense single strands.

In preferred embodiments, the subject S. pneumoniae nucleic acid willinclude a transcriptional regulatory sequence, e.g. at least one of atranscriptional promoter or transcriptional enhancer sequence, operablylinked to the S. pneumoniae gene sequence, e.g., to render the S.pneumoniae gene sequence suitable for expression in a recombinant hostcell.

In yet a further preferred embodiment, the nucleic acid which encodes anS. pneumoniae polypeptide of the invention, hybridizes under stringentconditions to a nucleic acid probe corresponding to at least 8consecutive nucleotides of the invention contained in the SequenceListing; more preferably to at least 12 consecutive nucleotides of theinvention contained in the Sequence Listing; more preferably to at least20 consecutive nucleotides of the invention contained in the SequenceListing; more preferably to at least 40 consecutive nucleotides of theinvention contained in the Sequence Listing.

In another aspect, the invention provides a substantially pure nucleicacid having a nucleotide sequence which encodes an S. pneumoniaepolypeptide. In preferred embodiments: the encoded polypeptide hasbiological activity; the encoded polypeptide has an amino acid sequenceat least 60%, 70%, 80%, 90%, 95%, 98%, or 99% homologous to an aminoacid sequence of the invention contained in the Sequence Listing; theencoded polypeptide has an amino acid sequence essentially the same asan amino acid sequence of the invention contained in the SequenceListing; the encoded polypeptide is at least 5, 10, 20, 50, 100, or 150amino acids in length; the encoded polypeptide comprises at least 5,preferably at least 10, more preferably at least 20, more preferably atleast 50, 100, or 150 contiguous amino acids of the invention containedin the Sequence Listing.

In another aspect, the invention encompasses: a vector including anucleic acid which encodes an S. pneumoniae polypeptide or an S.pneumoniae polypeptide variant as described herein; a host celltransfected with the vector; and a method of producing a recombinant S.pneumoniae polypeptide or S. pneumoniae polypeptide variant; includingculturing the cell, e.g., in a cell culture medium, and isolating an S.pneumoniae polypeptide or an S. pneumoniae polypeptide variant, e.g.,from the cell or from the cell culture medium.

In another series of embodiments, the invention provides isolatednucleic acids comprising sequences at least about 8 nucleotides inlength, more preferably at least about 12 nucleotides in length, andmost preferably at least about 15-20 nucleotides in length, thatcorrespond to a subsequence of any one of SEQ ID NO: 1-SEQ ID NO: 2661or complements thereof. Alternatively, the nucleic acids comprisesequences contained within any ORF (open reading frame), including acomplete protein-coding sequence, of which any of SEQ ID NO: 1-SEQ IDNO: 2661 forms a part. The invention encompasses sequence-conservativevariants and function-conservative variants of these sequences. Thenucleic acids may be DNA, RNA, DNA/RNA duplexes, protein-nucleic acid(PNA), or derivatives thereof.

In another aspect, the invention features, a purified recombinantnucleic acid having at least 50%, 60%, 70%, 80%, 90%, 95%, 98%, or 99%homology with a sequence of the invention contained in the SequenceListing.

In another aspect, the invention features nucleic acids capable ofbinding mRNA of S. pneumoniae. Such nucleic acid is capable of acting asantisense nucleic acid to control the translation of mRNA of S.pneumoniae. A further aspect features a nucleic acid which is capable ofbinding specifically to an S. pneumoniae nucleic acid. These nucleicacids are also referred to herein as complements and have utility asprobes and as capture reagents.

In another aspect, the invention features an expression systemcomprising an open reading frame corresponding to S. pneumoniae nucleicacid. The nucleic acid further comprises a control sequence compatiblewith an intended host. The expression system is useful for makingpolypeptides corresponding to S. pneumoniae nucleic acid.

In another aspect, the invention features a cell transformed with theexpression system to produce S. pneumoniae polypeptides.

In yet another embodiment, the invention encompasses reagents fordetecting bacterial infection, including S. pneumoniae infection, whichcomprise at least one S. pneumoniae-derived nucleic acid defined by anyone of SEQ ID NO: 1-SEQ ID NO: 2661, or sequence-conservative orfunction-conservative variants thereof. Alternatively, the diagnosticreagents comprise polypeptide sequences that are contained within anyopen reading frames (ORFs), including complete protein-coding sequences,contained within any of SEQ ID NO: 1-SEQ ID NO: 2661, or polypeptidesequences contained within any of SEQ ID NO: 2662-SEQ ID NO: 5322, orpolypeptides of which any of the above sequences forms a part, orantibodies directed against any of the above peptide sequences orfunction-conservative variants and/or fragments thereof.

The invention further provides antibodies, preferably monoclonalantibodies, which specifically bind to the polypeptides of theinvention. Methods are also provided for producing antibodies in a hostanimal. The methods of the invention comprise immunizing an animal withat least one S. pneumoniae-derived immunogenic component, wherein theimmunogenic component comprises one or more of the polypeptides encodedby any one of SEQ ID NO: 1-SEQ ID NO: 2661 or sequence-conservative orfunction-conservative variants thereof; or polypeptides that arecontained within any ORFs, including complete protein-coding sequences,of which any of SEQ ID NO: 1-SEQ ID NO: 2661 forms a part; orpolypeptide sequences contained within any of SEQ ID NO: 2662-SEQ ID NO:5322; or polypeptides of which any of SEQ ID NO: 2662-SEQ ID NO: 5322forms a part. Host animals include any warm blooded animal, includingwithout limitation mammals and birds. Such antibodies have utility asreagents for immunoassays to evaluate the abundance and distribution ofS. pneumoniae-specific antigens.

In yet another aspect, the invention provides a method for detectingbacterial antigenic components in a sample, which comprises the stepsof: (i) contacting a sample suspected to contain a bacterial antigeniccomponent with a bacterial-specific antibody, under conditions in whicha stable antigen-antibody complex can form between the antibody andbacterial antigenic components in the sample; and (ii) detecting anyantigen-antibody complex formed in step (i), wherein detection of anantigen-antibody complex indicates the presence of at least onebacterial antigenic component in the sample. In different embodiments ofthis method, the antibodies used are directed against a sequence encodedby any of SEQ ID NO: 1-SEQ ID NO: 2661 or sequence-conservative orfunction-conservative variants thereof, or against a polypeptidesequence contained in any of SEQ ID NO: 2662-SEQ ID NO: 5322 orfunction-conservative variants thereof.

In yet another aspect, the invention provides a method for detectingantibacterial-specific antibodies in a sample, which comprises: (i)contacting a sample suspected to contain antibacterial-specificantibodies with a S. pneumoniae antigenic component, under conditions inwhich a stable antigen-antibody complex can form between the S.pneumoniae antigenic component and antibacterial antibodies in thesample; and (ii) detecting any antigen-antibody complex formed in step(i), wherein detection of an antigen-antibody complex indicates thepresence of antibacterial antibodies in the sample. In differentembodiments of this method, the antigenic component is encoded by asequence contained in any of SEQ ID NO: 1-SEQ ID NO: 2661 orsequence-conservative and function-conservative variants thereof, or isa polypeptide sequence contained in any of SEQ ID NO: 2662-SEQ ID NO:5322 or function-conservative variants thereof.

In another aspect, the invention features a method of generatingvaccines for immunizing an individual against S. pneumoniae. The methodincludes: immunizing a subject with an S. pneumoniae polypeptide, e.g.,a surface or secreted polypeptide, or active portion thereof, and apharmaceutically acceptable carrier. Such vaccines have therapeutic andprophylactic utilities.

In another aspect, the invention features a method of evaluating acompound, e.g. a polypeptide, e.g., a fragment of a host cellpolypeptide, for the ability to bind an S. pneumoniae polypeptide. Themethod includes: contacting the candidate compound with an S. pneumoniaepolypeptide and determining if the compound binds or otherwise interactswith an S. pneumoniae polypeptide. Compounds which bind S. pneumoniaeare candidates as activators or inhibitors of the bacterial life cycle.These assays can be performed in vitro or in vivo.

In another aspect, the invention features a method of evaluating acompound, e.g. a polypeptide, e.g., a fragment of a host cellpolypeptide, for the ability to bind an S. pneumoniae nucleic acid,e.g., DNA or RNA. The method includes: contacting the candidate compoundwith an S. pneumoniae nucleic acid and determining if the compound bindsor otherwise interacts with an S. pneumoniae polypeptide. Compoundswhich bind S. pneumoniae are candidates as activators or inhibitors ofthe bacterial life cycle. These assays can be performed in vitro or invivo.

DETAILED DESCRIPTION OF THE INVENTION

The sequences of the present invention include the specific nucleic acidand amino acid sequences set forth in the Sequence Listing that forms apart of the present specification, and which are designated SEQ ID NO:1-SEQ ID NO: 5322. Use of the terms “SEQ ID NO: 1-SEQ ID NO: 2661”, “SEQID NO: 2662-SEQ ID NO: 5322”, “the sequences depicted in Table 2”, etc.,is intended, for convenience, to refer to each individual SEQ ID NOindividually, and is not intended to refer to the genus of thesesequences. In other words, it is a shorthand for listing all of thesesequences individually. The invention encompasses each sequenceindividually, as well as any combination thereof.

DEFINITIONS

“Nucleic acid” or “polynucleotide” as used herein refers to purine- andpyrimidine-containing polymers of any length, either polyribonucleotidesor polydeoxyribonucleotides or mixed polyribo-polydeoxyribo nucleotides.This includes single- and double-stranded molecules, i.e., DNA-DNA,DNA-RNA and RNA-RNA hybrids, as well as “protein nucleic acids” (PNA)formed by conjugating bases to an amino acid backbone. This alsoincludes nucleic acids containing modified bases.

A nucleic acid or polypeptide sequence that is “derived from” adesignated sequence refers to a sequence that corresponds to a region ofthe designated sequence. For nucleic acid sequences, this encompassessequences that are homologous or complementary to the sequence, as wellas “sequence-conservative variants” and “function-conservativevariants.” For polypeptide sequences, this encompasses“function-conservative variants.” Sequence-conservative variants arethose in which a change of one or more nucleotides in a given codonposition results in no alteration in the amino acid encoded at thatposition. Function-conservative variants are those in which a givenamino acid residue in a polypeptide has been changed without alteringthe overall conformation and function of the native polypeptide,including, but not limited to, replacement of an amino acid with onehaving similar physico-chemical properties (such as, for example,acidic, basic, hydrophobic, and the like).“Function-conservative”variants also include any polypeptides that havethe ability to elicit antibodies specific to a designated polypeptide.

An “S. pneumoniae-derived” nucleic acid or polypeptide sequence may ormay not be present in other bacterial species, and may or may not bepresent in all S. pneumoniae strains. This term is intended to refer tothe source from which the sequence was originally isolated. Thus, a S.pneumoniae-derived polypeptide, as used herein, may be used, e.g., as atarget to screen for a broad spectrum antibacterial agent, to search forhomologous proteins in other species of bacteria or in eukaryoticorganisms such as fungi and humans, etc.

A purified or isolated polypeptide or a substantially pure preparationof a polypeptide are used interchangeably herein and, as used herein,mean a polypeptide that has been separated from other proteins, lipids,and nucleic acids with which it naturally occurs. Preferably, thepolypeptide is also separated from substances, e.g., antibodies or gelmatrix, e.g., polyacrylamide, which are used to purify it. Preferably,the polypeptide constitutes at least 10, 20, 50 70, 80 or 95% dry weightof the purified preparation. Preferably, the preparation contains:sufficient polypeptide to allow protein sequencing; at least 1, 10, or100 mg of the polypeptide.

A purified preparation of cells refers to, in the case of plant oranimal cells, an in vitro preparation of cells and not an entire intactplant or animal. In the case of cultured cells or microbial cells, itconsists of a preparation of at least 10% and more preferably 50% of thesubject cells.

A purified or isolated or a substantially pure nucleic acid, e.g., asubstantially pure DNA, (are terms used interchangeably herein) is anucleic acid which is one or both of the following: not immediatelycontiguous with both of the coding sequences with which it isimmediately contiguous (i.e., one at the 5′ end and one at the 3′ end)in the naturally-occurring genome of the organism from which the nucleicacid is derived; or which is substantially free of a nucleic acid withwhich it occurs in the organism from which the nucleic acid is derived.The term includes, for example, a recombinant DNA which is incorporatedinto a vector, e.g., into an autonomously replicating plasmid or virus,or into the genomic DNA of a prokaryote or eukaryote, or which exists asa separate molecule (e.g., a cDNA or a genomic DNA fragment produced byPCR or restriction endonuclease treatment) independent of other DNAsequences. Substantially pure DNA also includes a recombinant DNA whichis part of a hybrid gene encoding additional S. pneumoniae DNA sequence.

A “contig” as used herein is a nucleic acid representing a continuousstretch of genomic sequence of an organism.

An “open reading frame”, also referred to herein as ORF, is a region ofnucleic acid which encodes a polypeptide. This region usually representsthe total coding region for the polypeptide and can be determined from astop to stop codon or from a start to stop codon.

As used herein, a “coding sequence” is a nucleic acid which istranscribed into messenger RNA and/or translated into a polypeptide whenplaced under the control of appropriate regulatory sequences. Theboundaries of the coding sequence are determined by a translation startcodon at the five prime terminus and a translation stop codon at thethree prime terminus. A coding sequence can include but is not limitedto messenger RNA, synthetic DNA, and recombinant nucleic acid sequences.

A “complement” of a nucleic acid as used herein refers to ananti-parallel or antisense sequence that participates in Watson-Crickbase-pairing with the original sequence.

A “gene product” is a protein or structural RNA which is specificallyencoded by a gene.

As used herein, the term “probe” refers to a nucleic acid, peptide orother chemical entity which specifically binds to a molecule ofinterest. Probes are often associated with or capable of associatingwith a label. A label is a chemical moiety capable of detection. Typicallabels comprise dyes, radioisotopes, luminescent and chemiluminescentmoieties, fluorophores, enzymes, precipitating agents, amplificationsequences, and the like. Similarly, a nucleic acid, peptide or otherchemical entity which specifically binds to a molecule of interest andimmobilizes such molecule is referred herein as a “capture ligand”.Capture ligands are typically associated with or capable of associatingwith a support such as nitro-cellulose, glass, nylon membranes, beads,particles and the like. The specificity of hybridization is dependent onconditions such as the base pair composition of the nucleotides, and thetemperature and salt concentration of the reaction. These conditions arereadily discernable to one of ordinary skill in the art using routineexperimentation.

“Homologous” refers to the sequence similarity or sequence identitybetween two polypeptides or between two nucleic acid molecules. When aposition in both of the two compared sequences is occupied by the samebase or amino acid monomer subunit, e.g., if a position in each of twoDNA molecules is occupied by adenine, then the molecules are homologousat that position. The percent of homology between two sequences is afunction of the number of matching or homologous positions shared by thetwo sequences divided by the number of positions compared×100. Forexample, if 6 of 10 of the positions in two sequences are matched orhomologous then the two sequences are 60% homologous. By way of example,the DNA sequences ATTGCC and TATGGC share 50% homology. Generally, acomparison is made when two sequences are aligned to give maximumhomology.

Nucleic acids are hybridizable to each other when at least one strand ofa nucleic acid can anneal to the other nucleic acid under definedstringency conditions. Stringency of hybridization is determined by: (a)the temperature at which hybridization and/or washing is performed; and(b) the ionic strength and polarity of the hybridization and washingsolutions. Hybridization requires that the two nucleic acids containcomplementary sequences; depending on the stringency of hybridization,however, mismatches may be tolerated. Typically, hybridization of twosequences at high stringency (such as, for example, in a solution of0.5×SSC, at 65° C.) requires that the sequences be essentiallycompletely homologous. Conditions of intermediate stringency (such as,for example, 2×SSC at 65° C.) and low stringency (such as, for example2×SSC at 55° C.), require correspondingly less overall complementaritybetween the hybridizing sequences. (1×SSC is 0.15 M NaCl, 0.015 M Nacitrate).

The terms peptides, proteins, and polypeptides are used interchangeablyherein.

As used herein, the term “surface protein” refers to all surfaceaccessible proteins, e.g. inner and outer membrane proteins, proteinsadhering to the cell wall, and secreted proteins.

A polypeptide has S. pneumoniae biological activity if it has one, twoand preferably more of the following properties: (1) if when expressedin the course of an S. pneumoniae infection, it can promote, or mediatethe attachment of S. pneumoniae to a cell; (2) it has an enzymaticactivity, structural or regulatory function characteristic of an S.pneumoniae protein; (3) or the gene which encodes it can rescue a lethalmutation in an S. pneumoniae gene. A polypeptide has biological activityif it is an antagonist, agonist, or super-agonist of a polypeptidehaving one of the above-listed properties.

A biologically active fragment or analog is one having an in vivo or invitro activity which is characteristic of the S. pneumoniae polypeptidesof the invention contained in the Sequence Listing, or of othernaturally occurring S. pneumoniae polypeptides, e.g., one or more of thebiological activities described herein. Especially preferred arefragments which exist in vivo, e.g., fragments which arise from posttranscriptional processing or which arise from translation ofalternatively spliced RNA's. Fragments include those expressed in nativeor endogenous cells as well as those made in expression systems, e.g.,in CHO cells. Because peptides such as S. pneumoniae polypeptides oftenexhibit a range of physiological properties and because such propertiesmay be attributable to different portions of the molecule, a useful S.pneumoniae fragment or S. pneumoniae analog is one which exhibits abiological activity in any biological assay for S. pneumoniae activity.Most preferably the fragment or analog possesses 10%, preferably 40%,more preferably 60%, 70%, 80% or 90% or greater of the activity of S.pneumoniae, in any in vivo or in vitro assay.

Analogs can differ from naturally occurring S. pneumoniae polypeptidesin amino acid sequence or in ways that do not involve sequence, or both.Non-sequence modifications include changes in acetylation, methylation,phosphorylation, carboxylation, or glycosylation. Preferred analogsinclude S. pneumoniae polypeptides (or biologically active fragmentsthereof) whose sequences differ from the wild-type sequence by one ormore conservative amino acid substitutions or by one or morenon-conservative amino acid substitutions, deletions, or insertionswhich do not substantially diminish the biological activity of the S.pneumoniae polypeptide. Conservative substitutions typically include thesubstitution of one amino acid for another with similar characteristics,e.g., substitutions within the following groups: valine, glycine;glycine, alanine; valine, isoleucine, leucine; aspartic acid, glutamicacid; asparagine, glutamine; serine, threonine; lysine, arginine; andphenylalanine, tyrosine. Other conservative substitutions can be made inview of the table below.

TABLE 1 CONSERVATIVE AMINO ACID REPLACEMENTS For Amino Acid Code Replacewith any of Alanine A D-Ala, Gly, beta-Ala, L-Cys, D-Cys Arginine RD-Arg, Lys, D-Lys, homo-Arg, D-homo-Arg, Met, Ile, D-Met, D-Ile, Orn,D-Orn Asparagine N D-Asn, Asp, D-Asp, Glu, D-Glu, Gln, D-Gln AsparticAcid D D-Asp, D-Asn, Asn, Glu, D-Glu, Gln, D-Gln Cysteine C D-Cys,S—Me-Cys, Met, D-Met, Thr, D-Thr Glutamine Q D-Gln, Asn, D-Asn, Glu,D-Glu, Asp, D-Asp Glutamic Acid E D-Glu, D-Asp, Asp, Asn, D-Asn, Gln,D-Gln Glycine G Ala, D-Ala, Pro, D-Pro, β-Ala, Acp Isoleucine I D-Ile,Val, D-Val, Leu, D-Leu, Met, D-Met Leucine L D-Leu, Val, D-Val, Leu,D-Leu, Met, D-Met Lysine K D-Lys, Arg, D-Arg, homo-Arg, D-homo-Arg, Met,D-Met, Ile, D-Ile, Orn, D-Orn Methionine M D-Met, S—Me-Cys, Ile, D-Ile,Leu, D-Leu, Val, D-Val Phenylalanine F D-Phe, Tyr, D-Thr, L-Dopa, His,D-His, Trp, D-Trp, Trans-3,4, or 5-phenylproline, cis-3,4, or5-phenylproline Proline P D-Pro, L-I-thioazolidine-4-carboxylic acid,D-or L-1-oxazolidine-4-carboxylic acid Serine S D-Ser, Thr, D-Thr,allo-Thr, Met, D-Met, Met(O), D-Met(O), L-Cys, D-Cys Threonine T D-Thr,Ser, D-Ser, allo-Thr, Met, D-Met, Met(O), D-Met(O), Val, D-Val TyrosineY D-Tyr, Phe, D-Phe, L-Dopa, His, D-His Valine V D-Val, Leu, D-Leu, Ile,D-Ile, Met, D-Met

Other analogs within the invention are those with modifications whichincrease peptide stability; such analogs may contain, for example, oneor more non-peptide bonds (which replace the peptide bonds) in thepeptide sequence. Also included are: analogs that include residues otherthan naturally occurring L-amino acids, e.g., D-amino acids ornon-naturally occurring or synthetic amino acids, e.g., β or γ aminoacids; and cyclic analogs.

As used herein, the term “fragment”, as applied to an S. pneumoniaeanalog, will ordinarily be at least about 20 residues, more typically atleast about 40 residues, preferably at least about 60 residues inlength. Fragments of S. pneumoniae polypeptides can be generated bymethods known to those skilled in the art. The ability of a candidatefragment to exhibit a biological activity of S. pneumoniae polypeptidecan be assessed by methods known to those skilled in the art asdescribed herein. Also included are S. pneumoniae polypeptidescontaining residues that are not required for biological activity of thepeptide or that result from alternative mRNA splicing or alternativeprotein processing events.

An “immunogenic component” as used herein is a moiety, such as an S.pneumoniae polypeptide, analog or fragment thereof, that is capable ofeliciting a humoral and/or cellular immune response in a host animal.

An “antigenic component” as used herein is a moiety, such as an S.pneumoniae polypeptide, analog or fragment thereof, that is capable ofbinding to a specific antibody with sufficiently high affinity to form adetectable antigen-antibody complex.

The term “antibody” as used herein is intended to include fragmentsthereof which are specifically reactive with S. pneumoniae polypeptides.

As used herein, the term “cell-specific promoter” means a DNA sequencethat serves as a promoter, i.e., regulates expression of a selected DNAsequence operably linked to the promoter, and which effects expressionof the selected DNA sequence in specific cells of a tissue. The termalso covers so-called “leaky” promoters, which regulate expression of aselected DNA primarily in one tissue, but cause expression in othertissues as well.

Misexpression, as used herein, refers to a non-wild type pattern of geneexpression. It includes: expression at non-wild type levels, i.e., overor under expression; a pattern of expression that differs from wild typein terms of the time or stage at which the gene is expressed, e.g.,increased or decreased expression (as compared with wild type) at apredetermined developmental period or stage; a pattern of expressionthat differs from wild type in terms of decreased expression (ascompared with wild type) in a predetermined cell type or tissue type; apattern of expression that differs from wild type in terms of thesplicing size, amino acid sequence, post-translational modification, orbiological activity of the expressed polypeptide; a pattern ofexpression that differs from wild type in terms of the effect of anenvironmental stimulus or extracellular stimulus on expression of thegene, e.g., a pattern of increased or decreased expression (as comparedwith wild type) in the presence of an increase or decrease in thestrength of the stimulus.

As used herein, “host cells” and other such terms denotingmicroorganisms or higher eukaryotic cell lines cultured as unicellularentities refers to cells which can become or have been used asrecipients for a recombinant vector or other transfer DNA, and includethe progeny of the original cell which has been transfected. It isunderstood by individuals skilled in the art that the progeny of asingle parental cell may not necessarily be completely identical ingenomic or total DNA compliment to the original parent, due to accidentor deliberate mutation.

As used herein, the term “control sequence” refers to a nucleic acidhaving a base sequence which is recognized by the host organism toeffect the expression of encoded sequences to which they are ligated.The nature of such control sequences differs depending upon the hostorganism; in prokaryotes, such control sequences generally include apromoter, ribosomal binding site, terminators, and in some casesoperators; in eukaryotes, generally such control sequences includepromoters, terminators and in some instances, enhancers. The termcontrol sequence is intended to include at a minimum, all componentswhose presence is necessary for expression, and may also includeadditional components whose presence is advantageous, for example,leader sequences.

As used herein, the term “operably linked” refers to sequences joined orligated to function in their intended manner. For example, a controlsequence is operably linked to coding sequence by ligation in such a waythat expression of the coding sequence is achieved under conditionscompatible with the control sequence and host cell.

The “metabolism” of a substance, as used herein, means any aspect of theexpression, function, action, or regulation of the substance. Themetabolism of a substance includes modifications, e.g., covalent ornon-covalent modifications of the substance. The metabolism of asubstance includes modifications, e.g., covalent or non-covalentmodification, the substance induces in other substances. The metabolismof a substance also includes changes in the distribution of thesubstance. The metabolism of a substance includes changes the substanceinduces in the distribution of other substances.

A “sample” as used herein refers to a biological sample, such as, forexample, tissue or fluid isolated from an individual (including withoutlimitation plasma, serum, cerebrospinal fluid, lymph, tears, saliva andtissue sections) or from in vitro cell culture constituents, as well assamples from the environment.

Technical and scientific terms used herein have the meanings commonlyunderstood by one of ordinary skill in the art to which the presentinvention pertains, unless otherwise defined. Reference is made hereinto various methodologies known to those of skill in the art.Publications and other materials setting forth such known methodologiesto which reference is made are incorporated herein by reference in theirentireties as though set forth in full. The practice of the inventionwill employ, unless otherwise indicated, conventional techniques ofchemistry, molecular biology, microbiology, recombinant DNA, andimmunology, which are within the skill of the art. Such techniques areexplained fully in the literature. See e.g., Sambrook, Fritsch, andManiatis, Molecular Cloning; Laboratory Manual 2nd ed. (1989); DNACloning, Volumes I and II (D. N Glover ed. 1985); OligonucleotideSynthesis (M. J. Gait ed, 1984); Nucleic Acid Hybridization (B. D. Hames& S. J. Higgins eds. 1984); the series, Methods in Enzymoloqy (AcademicPress, Inc.), particularly Vol. 154 and Vol. 155 (Wu and Grossman,eds.); PCR—A Practical Approach (McPherson, Quirke, and Taylor, eds.,1991); Immunology, 2d Edition, 1989, Roitt et al., C.V. Mosby Company,and New York; Advanced Immunology, 2d Edition, 1991, Male et al., GrowerMedical Publishing, New York.; DNA Cloning: A Practical Approach,Volumes I and II, 1985 (D. N. Glover ed.); Oligonucleotide Synthesis,1984, (M. L. Gait ed); Transcription and Translation, 1984 (Hames andHiggins eds.); Animal Cell Culture, 1986 (R. I. Freshney ed.);Immobilized Cells and Enzymes, 1986 (IRL Press); Perbal, 1984, APractical Guide to Molecular Cloning; and Gene Transfer Vectors forMammalian Cells, 1987 (J. H. Miller and M. P. Calos eds., Cold SpringHarbor Laboratory).

Any suitable materials and/or methods known to those of skill can beutilized in carrying out the present invention: however preferredmaterials and/or methods are described. Materials, reagents and the liketo which reference is made in the following description and examples areobtainable from commercial sources, unless otherwise noted.

S. pneumoniae Genomic Sequence

This invention provides nucleotide sequences of the genome of S.pneumoniae which thus comprises a DNA sequence library of S. pneumoniaegenomic DNA. The detailed description that follows provides nucleotidesequences of S. pneumoniae, and also describes how the sequences wereobtained and how ORFs and protein-coding sequences were identified. Alsodescribed are methods of using the disclosed S. pneumoniae sequences inmethods including diagnostic and therapeutic applications. Furthermore,the library can be used as a database for identification and comparisonof medically important sequences in this and other strains of S.pneumoniae.

To determine the genomic sequence of S. pneumoniae, DNA was isolatedfrom strain 14453 of S. pneumoniae and mechanically sheared bynebulization to a median size of 2 kb. Following size fractionation bygel electrophoresis, the fragments were blunt-ended, ligated to adapteroligonucleotides, and cloned into each of 20 different pMPX vectors(Rice et al., abstracts of Meeting of Genome Mapping and Sequencing,Cold Spring Harbor, N.Y., 5/11-5/15, 1994, p. 225) and the PUC19 vectorto construct a series of “shotgun” subclone libraries.

DNA sequencing was achieved using two sequencing methods. The firstmethod used multiplex sequencing procedures essentially as disclosed inChurch et al., 1988, Science 240:185; U.S. Pat. Nos. 4,942,124 and5,149,625). DNA was extracted from pooled cultures and subjected tochemical or enzymatic sequencing. Sequencing reactions were resolved byelectrophoresis, and the products were transferred and covalently boundto nylon membranes. Finally, the membranes were sequentially hybridizedwith a series of labelled oligonucleotides complimentary to “tag”sequences present in the different shotgun cloning vectors. In thismanner, a large number of sequences could be obtained from a single setof sequencing reactions. The remainder of the sequencing was performedon ABI377 automated DNA sequencers. The cloning and sequencingprocedures are described in more detail in the Exemplification.

Individual sequence reads were assembled using PHRAP (P. Green,Abstracts of DOE Human Genome Program Contractor-Grantee Workshop V,January 1996, p. 157). The average contig length was about 3-4 kb.

A variety of approaches are used to order the contigs so as to obtain acontinuous sequence representing the entire S. pneumoniae genome.Synthetic oligonucleotides are designed that are complementary tosequences at the end of each contig. These oligonucleotides may behybridized to libaries of S. pneumoniae genomic DNA in, for example,lambda phage vectors or plasmid vectors to identify clones that containsequences corresponding to the junctional regions between individualcontigs. Such clones are then used to isolate template DNA and the sameoligonucleotides are used as primers in polymerase chain reaction (PCR)to amplify junctional fragments, the nucleotide sequence of which isthen determined.

The S. pneumoniae sequences were analyzed for the presence of openreading frames (ORFs) comprising at least 180 nucleotides. As a resultof the initial analysis of ORFs based on stop-to-stop codon reads, itshould be understood that these ORFs may not correspond to the ORF of anaturally-occurring S. pneumoniae polypeptide. These ORFs may containstart codons which indicate the initiation of protein synthesis of anaturally-occurring S. pneumoniae polypeptide. Such start codons withinthe ORFs provided herein can be identified by those of ordinary skill inthe relevant art, and the resulting ORF and the encoded S. pneumoniaepolypeptide is within the scope of this invention. For example, withinthe ORFs a codon such as AUG or GUG (encoding methionine or valine)which is part of the initiation signal for protein synthesis can beidentified and the portion of an ORF to corresponding to anaturally-occurring S. pneumoniae polypeptide can be recognized.

The second analysis of the ORFs included identifying the start codonsand the predicted coding regions. These ORFs provided in this inventionwere defined by one or more of the following methods: evaluating thecoding potential of such sequences with the program GENEMARK™(Borodovsky and McIninch, 1993, Comp. 17:123), distinguishing the codingfrom noncoding regions using the program Glimmer (Fraser et al, Nature,1997), determining codon usage (Staden et al., Nucleic Acid Research 10:141), and each predicted ORF amino acid sequence was compared with allprotein sequences found in current GENBANK, SWISS-PROT, and PIRdatabases using the BLAST algorithm. BLAST identifies local alignmentsoccurring by chance between the ORF sequence and the sequence in thedatabank (Altschal et al., 1990, L Mol. Biol. 215:403-410). HomologousORFs (probabilities less than 10⁻⁵ by chance) and ORF's that areprobably non-homologous (probabilities greater than 10⁻⁵ by chance) buthave good codon usage were identified. Both homologous, sequences andnon-homologous sequences with good codon usage are likely to encodeproteins and are encompassed by the invention.

S. pneumoniae Nucleic Acids

The nucleic acids of this invention may be obtained directly from theDNA of the above referenced S. pneumoniae strain by using the polymerasechain reaction (PCR). See “PCR, A Practical Approach” (McPherson,Quirke, and Taylor, eds., IRL Press, Oxford, UK, 1991) for details aboutthe PCR. High fidelity PCR can be used to ensure a faithful DNA copyprior to expression. In addition, the authenticity of amplified productscan be verified by conventional sequencing methods. Clones carrying thedesired sequences described in this invention may also be obtained byscreening the libraries by means of the PCR or by hybridization ofsynthetic oligonucleotide probes to filter lifts of the library coloniesor plaques as known in the art (see, e.g., Sambrook et al., MolecularCloning, A Laboratory Manual 2nd edition, 1989, Cold Spring HarborPress, NY).

It is also possible to obtain nucleic acids encoding S. pneumoniaepolypeptides from a cDNA library in accordance with protocols hereindescribed. A cDNA encoding an S. pneumoniae polypeptide can be obtainedby isolating total mRNA from an appropriate strain. Double strandedcDNAs can then be prepared from the total mRNA. Subsequently, the cDNAscan be inserted into a suitable plasmid or viral (e.g., bacteriophage)vector using any one of a number of known techniques. Genes encoding S.pneumoniae polypeptides can also be cloned using established polymerasechain reaction techniques in accordance with the nucleotide sequenceinformation provided by the invention. The nucleic acids of theinvention can be DNA or RNA. Preferred nucleic acids of the inventionare contained in the Sequence Listing.

The nucleic acids of the invention can also be chemically synthesizedusing standard techniques. Various methods of chemically synthesizingpolydeoxynucleotides are known, including solid-phase synthesis which,like peptide synthesis, has been fully automated in commerciallyavailable DNA synthesizers (See e.g., Itakura et al. U.S. Pat. No.4,598,049; Caruthers et al. U.S. Pat. No. 4,458,066; and Itakura U.S.Pat. Nos. 4,401,796 and 4,373,071, incorporated by reference herein).

Nucleic acids isolated or synthesized in accordance with features of thepresent invention are useful, by way of example, without limitation, asprobes, primers, capture ligands, antisense genes and for developingexpression systems for the synthesis of proteins and peptidescorresponding to such sequences. As probes, primers, capture ligands andantisense agents, the nucleic acid normally consists of all or part(approximately twenty or more nucleotides for specificity as well as theability to form stable hybridization products) of the nucleic acids ofthe invention contained in the Sequence Listing. These uses aredescribed in further detail below.

Probes

A nucleic acid isolated or synthesized in accordance with the sequenceof the invention contained in the Sequence Listing can be used as aprobe to specifically detect S. pneumoniae. With the sequenceinformation set forth in the present application, sequences of twenty ormore nucleotides are identified which provide the desired inclusivityand exclusivity with respect to S. pneumoniae, and extraneous nucleicacids likely to be encountered during hybridization conditions. Morepreferably, the sequence will comprise at least twenty to thirtynucleotides to convey stability to the hybridization product formedbetween the probe and the intended target molecules.

Sequences larger than 1000 nucleotides in length are difficult tosynthesize but can be generated by recombinant DNA techniques.Individuals skilled in the art will readily recognize that the nucleicacids, for use as probes, can be provided with a label to facilitatedetection of a hybridization product.

Nucleic acid isolated and synthesized in accordance with the sequence ofthe invention contained in the Sequence Listing can also be useful asprobes to detect homologous regions (especially homologous genes) ofother Streptococcus species using appropriate stringency hybridizationconditions as described herein.

Capture Ligand

For use as a capture ligand, the nucleic acid selected in the mannerdescribed above with respect to probes, can be readily associated with asupport. The manner in which nucleic acid is associated with supports iswell known. Nucleic acid having twenty or more nucleotides in a sequenceof the invention contained in the Sequence Listing have utility toseparate S. pneumoniae nucleic acid from the nucleic acid of each otherand other organisms. Nucleic acid having twenty or more nucleotides in asequence of the invention contained in the Sequence Listing can alsohave utility to separate other Streptococcus species from each other andfrom other organisms. Preferably, the sequence will comprise at leasttwenty nucleotides to convey stability to the hybridization productformed between the probe and the intended target molecules. Sequenceslarger than 1000 nucleotides in length are difficult to synthesize butcan be generated by recombinant DNA techniques.

Primers

Nucleic acid isolated or synthesized in accordance with the sequencesdescribed herein have utility as primers for the amplification of S.pneumoniae nucleic acid. These nucleic acids may also have utility asprimers for the amplification of nucleic acids in other Streptococcusspecies. With respect to polymerase chain reaction (PCR) techniques,nucleic acid sequences of ≧10-15 nucleotides of the invention containedin the Sequence Listing have utility in conjunction with suitableenzymes and reagents to create copies of S. pneumoniae nucleic acid.More preferably, the sequence will comprise twenty or more nucleotidesto convey stability to the hybridization product formed between theprimer and the intended target molecules. Binding conditions of primersgreater than 100 nucleotides are more difficult to control to obtainspecificity. High fidelity PCR can be used to ensure a faithful DNA copyprior to expression. In addition, amplified products can be checked byconventional sequencing methods.

The copies can be used in diagnostic assays to detect specificsequences, including genes from S. pneumoniae and/or other Streptococcusspecies. The copies can also be incorporated into cloning and expressionvectors to generate polypeptides corresponding to the nucleic acidsynthesized by PCR, as is described in greater detail herein.

Antisense

Nucleic acid or nucleic acid-hybridizing derivatives isolated orsynthesized in accordance with the sequences described herein haveutility as antisense agents to prevent the expression of S. pneumoniaegenes. These sequences also have utility as antisense agents to preventexpression of genes of other Streptococcus species.

In one embodiment, nucleic acid or derivatives corresponding to S.pneumoniae nucleic acids is loaded into a suitable carrier such as aliposome or bacteriophage for introduction into bacterial cells. Forexample, a nucleic acid having twenty or more nucleotides is capable ofbinding to bacteria nucleic acid or bacteria messenger RNA. Preferably,the antisense nucleic acid is comprised of 20 or more nucleotides toprovide necessary stability of a hybridization product of non-naturallyoccurring nucleic acid and bacterial nucleic acid and/or bacterialmessenger RNA. Nucleic acid having a sequence greater than 1000nucleotides in length is difficult to synthesize but can be generated byrecombinant DNA techniques. Methods for loading antisense nucleic acidin liposomes is known in the art as exemplified by U.S. Pat. No.4,241,046 issued Dec. 23, 1980 to Papahadjopoulos et al.

The present invention encompasses isolated polypeptides and nucleicacids derived from S. pneumoniae that are useful as reagents fordiagnosis of bacterial infection, components of effective antibacterialvaccines, and/or as targets for antibacterial drugs, including anti-S.pneumoniae drugs.

Expression of S. pneumoniae Nucleic Acids

Table 2 provides a list of open reading frames (ORFs) in both strands.An ORF is a region of nucleic acid which encodes a polypeptide. Thisregion normally represents a complete coding sequence or a totalsequence and was determined from an initial analysis of stop to stopcodons followed by the prediction of start codons. The first columnlists the ORF designation. The second and third columns list the SEQ IDnumbers for the nucleic acid and amino acid sequences corresponding toeach ORF, respectively. The fourth and fifth columns list the length ofthe nucleic acid ORF and the length of the amino acid ORF, respectively.Most of the nucleotide sequences corresponding to each ORF begin at thefirst nucleotide of the start codon and end at the nucleotideimmediately preceding the next downstream stop codon in the same readingframe. It will be recognized by one skilled in the art that the naturaltranslation initiation sites will correspond to ATG, GTG, or TTG codonslocated within the ORFs. The natural initiation sites depend not only onthe sequence of a start codon but also on the context of the DNAsequence adjacent to the start codon. Usually, a recognizable ribosomebinding site is found within 20 nucleotides upstream from the initiationcodon. In some cases where genes are translationally coupled andcoordinately expressed together in “operons”, ribosome binding sites arenot present, but the initiation codon of a downstream gene may occurvery close to, or overlap, the stop codon of the an upstream gene in thesame operon. The correct start codons can be generally identifiedrapidly and efficiently because only a few codons need be tested. It isrecognized that the translational machinery in bacteria initiates mostpolypeptide chains with the amino acid methionine. In some cases,polypeptides are post-translationally modified, resulting in anN-terminal amino acid other than methionine in vivo. The sixth andseventh columns provide metrics for assessing the likelihood of thehomology match (determined by the BLASTP2 algorithm), as is known in theart, to the genes indicated in the description field. Specifically, thesixth column represents the “Score” for the match (a higher score is abetter match), and the seventh column represents the “P-value” for thematch (the probability that such a match could have occurred by chance;the lower the value, the more likely the match is valid). If a BLASTP2score of less than 46 was obtained, no value is reported in the tablethe “P-value”. The description field provides, where available, theaccession number (AC) or the Swissprot accession number (SP), the locusname (LN), Superfamily Classification (CL), the Organism (OR), Source ofvariant (SR), E.C. number (EC), the gene name (GN), the product name(PN), the Function Description (FN), the Map Position (MP), Left End(LE), Right End (RE), Coding Direction (DI), the Database from which thesequence originates (DB), and the description (DE) or notes (NT) foreach ORF. This information allows one of ordinary skill in the art todetermine a potential use and function for each identified codingsequence and, as a result, allows the use of the polypeptides of thepresent invention for commercial and industrial purposes.

Using the information provided in SEQ ID NO: 1-SEQ ID NO: 2661 and inTable 2 together with routine cloning and sequencing methods, one ofordinary skill in the art will be able to clone and sequence all thenucleic acid fragments of interest including open reading frames (ORFs)encoding a large variety proteins of S. pneumoniae.

Nucleic acid isolated or synthesized in accordance with the sequencesdescribed herein have utility to generate polypeptides. The nucleic acidof the invention exemplified in SEQ ID NO: 1-SEQ ID NO: 2661 and inTable 2 or fragments of said nucleic acid encoding active portions of S.pneumoniae polypeptides can be cloned into suitable vectors or used toisolate nucleic acid. The isolated nucleic acid is combined withsuitable DNA linkers and cloned into a suitable vector.

The function of a specific gene or operon can be ascertained byexpression in a bacterial strain under conditions where the activity ofthe gene product(s) specified by the gene or operon in question can bespecifically measured. Alternatively, a gene product may be produced inlarge quantities in an expressing strain for use as an antigen, anindustrial reagent, for structural studies, etc. This expression can beaccomplished in a mutant strain which lacks the activity of the gene tobe tested, or in a strain that does not produce the same geneproduct(s). This includes, but is not limited to, Eucaryotic speciessuch as the yeast Saccharomyces cerevisiae, Methanobacterium strains orother Archaea, and Eubacteria such as E. coli, B. subtilis, S. aureus,S. pneumonia or Pseudomonas putida. In some cases the expression hostwill utilize the natural S. pneumoniae promoter whereas in others, itwill be necessary to drive the gene with a promoter sequence derivedfrom the expressing organism (e.g., an E. coli beta-galactosidasepromoter for expression in E. coli).

To express a gene product using the natural S. pneumoniae promoter, aprocedure such as the following can be used. A restriction fragmentcontaining the gene of interest, together with its associated naturalpromoter element and regulatory sequences (identified using the DNAsequence data) is cloned into an appropriate recombinant plasmidcontaining an origin of replication that functions in the host organismand an appropriate selectable marker. This can be accomplished by anumber of procedures known to those skilled in the art. It is mostpreferably done by cutting the plasmid and the fragment to be clonedwith the same restriction enzyme to produce compatible ends that can beligated to join the two pieces together. The recombinant plasmid isintroduced into the host organism by, for example, electroporation andcells containing the recombinant plasmid are identified by selection forthe marker on the plasmid. Expression of the desired gene product isdetected using an assay specific for that gene product.

In the case of a gene that requires a different promoter, the body ofthe gene (coding sequence) is specifically excised and cloned into anappropriate expression plasmid. This subcloning can be done by severalmethods, but is most easily accomplished by PCR amplification of aspecific fragment and ligation into an expression plasmid after treatingthe PCR product with a restriction enzyme or exonuclease to createsuitable ends for cloning.

A suitable host cell for expression of a gene can be any procaryotic oreucaryotic cell. For example, an S. pneumoniae polypeptide can beexpressed in bacterial cells such as E. coli or B. subtilis, insectcells (baculovirus), yeast, or mammalian cells such as Chinese hamsterovary cell (CHO). Other suitable host cells are known to those skilledin the art.

Expression in eucaryotic cells such as mammalian, yeast, or insect cellscan lead to partial or complete glycosylation and/or formation ofrelevant inter- or intra-chain disulfide bonds of a recombinant peptideproduct. Examples of vectors for expression in yeast S. cerivisaeinclude pYepSec1 (Baldari. et al., (1987) Embo J. 6:229-234), pMFa(Kurjan and Herskowitz, (1982) Cell 30:933-943), pJRY88 (Schultz et al.,(1987) Gene 54:113-123), and pYES2 (Invitrogen Corporation, San Diego,Calif.). Baculovirus vectors available for expression of proteins incultured insect cells (SF 9 cells) include the pAc series (Smith et al.,(1983) Mol. Cell Biol. 3:2156-2165) and the pVL series (Lucklow, V. A.,and Summers, M. D., (1989) Virology 170:31-39). Generally, COS cells(Gluzman, Y., (1981) Cell 23:175-182) are used in conjunction with suchvectors as pCDM 8 (Aruffo, A. and Seed, B., (1987) Proc. Natl. Acad.Sci. USA 84:8573-8577) for transient amplification/expression inmammalian cells, while CHO (dhfr⁻ Chinese Hamster Ovary) cells are usedwith vectors such as pMT2PC (Kaufman et al. (1987), EMBO J. 6:187-195)for stable amplification/expression in mammalian cells. Vector DNA canbe introduced into mammalian cells via conventional techniques such ascalcium phosphate or calcium chloride co-precipitation,DEAE-dextran-mediated transfection, or electroporation. Suitable methodsfor transforming host cells can be found in Sambrook et al. (MolecularCloning: A Laboratory Manual, 2nd Edition, Cold Spring Harbor Laboratorypress (1989)), and other laboratory textbooks.

Expression in procaryotes is most often carried out in E. Coli witheither fusion or non-fusion inducible expression vectors. Fusion vectorsusually add a number of NH₂ terminal amino acids to the expressed targetgene. These NH₂ terminal amino acids often are referred to as a reportergroup or an affinity purification group. Such reporter groups usuallyserve two purposes: 1) to increase the solubility of the targetrecombinant protein; and 2) to aid in the purification of the targetrecombinant protein by acting as a ligand in affinity purification.Often, in fusion expression vectors, a proteolytic cleavage site isintroduced at the junction of the reporter group and the targetrecombinant protein to enable separation of the target recombinantprotein from the reporter group subsequent to purification of the fusionprotein. Such enzymes, and their cognate recognition sequences, includeFactor Xa, thrombin and enterokinase. Typical fusion expression vectorsinclude pGEX (Amrad Corp., Melbourne, Australia), pMAL (New EnglandBiolabs, Beverly, Mass.) and pRIT5 (Pharmacia, Piscataway, N.J.) whichfuse glutathione S-transferase, maltose E binding protein, or protein A,respectively, to the target recombinant protein. A preferred reportergroup is poly(His), which may be fused to the amino or carboxy terminusof the protein and which renders the recombinant fusion protein easilypurifiable by metal chelate chromatography.

Inducible non-fusion expression vectors include pTrc (Amann et al.,(1988) Gene 69:301-315) and pET11d (Studier et al., Gene ExpressionTechnology: Methods in Enzymology 185, Academic Press, San Diego, Calif.(1990) 60-89). While target gene expression relies on host RNApolymerase transcription from the hybrid trp-lac fusion promoter inpTrc, expression of target genes inserted into pET11d relies ontranscription from the T7 gn10-lac 0 fusion promoter mediated bycoexpressed viral RNA polymerase (T7 gn1). This viral polymerase issupplied by host strains BL21 (DE3) or HMS174(DE3) from a resident λprophage harboring a T7 gn1 under the transcriptional control of thelacUV 5 promoter.

For example, a host cell transfected with a nucleic acid vectordirecting expression of a nucleotide sequence encoding an S. pneumoniaepolypeptide can be cultured under appropriate conditions to allowexpression of the polypeptide to occur. The polypeptide may be secretedand isolated from a mixture of cells and medium containing the peptide.Alternatively, the polypeptide may be retained cytoplasmically and thecells harvested, lysed and the protein isolated. A cell culture includeshost cells, media and other byproducts. Suitable media for cell cultureare well known in the art. Polypeptides of the invention can be isolatedfrom cell culture medium, host cells, or both using techniques known inthe art for purifying proteins including ion-exchange chromatography,gel filtration chromatography, ultrafiltration, electrophoresis, andimmunoaffinity purification with antibodies specific for suchpolypeptides. Additionally, in many situations, polypeptides can beproduced by chemical cleavage of a native protein (e.g., trypticdigestion) and the cleavage products can then be purified by standardtechniques.

In the case of membrane bound proteins, these can be isolated from ahost cell by contacting a membrane-associated protein fraction with adetergent forming a solubilized complex, where the membrane-associatedprotein is no longer entirely embedded in the membrane fraction and issolubilized at least to an extent which allows it to bechromatographically isolated from the membrane fraction. Severaldifferent criteria are used for choosing a detergent suitable forsolubilizing these complexes. For example, one property considered isthe ability of the detergent to solubilize the S. pneumoniae proteinwithin the membrane fraction at minimal denaturation of themembrane-associated protein allowing for the activity or functionalityof the membrane-associated protein to return upon reconstitution of theprotein. Another property considered when selecting the detergent is thecritical micelle concentration (CMC) of the detergent in that thedetergent of choice preferably has a high CMC value allowing for ease ofremoval after reconstitution. A third property considered when selectinga detergent is the hydrophobicity of the detergent. Typically,membrane-associated proteins are very hydrophobic and thereforedetergents which are also hydrophobic, e.g., the triton series, would beuseful for solubilizing the hydrophobic proteins. Another propertyimportant to a detergent can be the capability of the detergent toremove the S. pneumoniae protein with minimal protein-proteininteraction facilitating further purification. A fifth property of thedetergent which should be considered is the charge of the detergent. Forexample, if it is desired to use ion exchange resins in the purificationprocess then preferably detergent should be an uncharged detergent.Chromatographic techniques which can be used in the final purificationstep are known in the art and include hydrophobic interaction, lectinaffinity, ion exchange, dye affinity and immunoaffinity.

One strategy to maximize recombinant S. pneumoniae peptide expression inE. coli is to express the protein in a host bacteria with an impairedcapacity to proteolytically cleave the recombinant protein (Gottesman,S., Gene Expression Technology: Methods in Enzymology 185, AcademicPress, San Diego, Calif. (1990) 119-128). Another strategy would be toalter the nucleic acid encoding an S. pneumoniae peptide to be insertedinto an expression vector so that the individual codons for each aminoacid would be those preferentially utilized in highly expressed E. coliproteins (Wada et al., (1992) Nuc. Acids Res. 20:2111-2118). Suchalteration of nucleic acids of the invention can be carried out bystandard DNA synthesis techniques.

The nucleic acids of the invention can also be chemically synthesizedusing standard techniques. Various methods of chemically synthesizingpolydeoxynucleotides are known, including solid-phase synthesis which,like peptide synthesis, has been fully automated in commerciallyavailable DNA synthesizers (See, e.g., Itakura et al. U.S. Pat. No.4,598,049; Caruthers et al. U.S. Pat. No. 4,458,066; and Itakura U.S.Pat. Nos. 4,401,796 and 4,373,071, incorporated by reference herein).

The present invention provides a library of S. pneumoniae-derivednucleic acid sequences. The libraries provide probes, primers, andmarkers which can be used as markers in epidemiological studies. Thepresent invention also provides a library of S. pneumoniae-derivednucleic acid sequences which comprise or encode targets for therapeuticdrugs.

Nucleic acids comprising any of the sequences disclosed herein orsub-sequences thereof can be prepared by standard methods using thenucleic acid sequence information provided in SEQ ID NO: 1-SEQ ID NO:2661. For example, DNA can be chemically synthesized using, e.g., thephosphoramidite solid support method of Matteucci et al., 1981, J. Am.Chem. Soc. 103:3185, the method of Yoo et al., 1989, J. Biol. Chem.764:17078, or other well known methods. This can be done by sequentiallylinking a series of oligonucleotide cassettes comprising pairs ofsynthetic oligonucleotides, as described below.

Of course, due to the degeneracy of the genetic code, many differentnucleotide sequences can encode polypeptides having the amino acidsequences defined by SEQ ID NO: 2662-SEQ ID NO: 5322 or sub-sequencesthereof. The codons can be selected for optimal expression inprokaryotic or eukaryotic systems. Such degenerate variants are alsoencompassed by this invention.

Insertion of nucleic acids (typically DNAs) encoding the polypeptides ofthe invention into a vector is easily accomplished when the termini ofboth the DNAs and the vector comprise compatible restriction sites. Ifthis cannot be done, it may be necessary to modify the termini of theDNAs and/or vector by digesting back single-stranded DNA overhangsgenerated by restriction endonuclease cleavage to produce blunt ends, orto achieve the same result by filling in the single-stranded terminiwith an appropriate DNA polymerase.

Alternatively, any site desired may be produced, e.g., by ligatingnucleotide sequences (linkers) onto the termini. Such linkers maycomprise specific oligonucleotide sequences that define desiredrestriction sites. Restriction sites can also be generated by the use ofthe polymerase chain reaction (PCR). See, e.g., Saiki et al., 1988,Science 239:48. The cleaved vector and the DNA fragments may also bemodified if required by homopolymeric tailing.

In certain embodiments, the invention encompasses isolated nucleic acidfragments comprising all or part of the individual nucleic acidsequences disclosed herein. The fragments are at least about 8nucleotides in length, preferably at least about 12 nucleotides inlength, and most preferably at least about 15-20 nucleotides in length.

The nucleic acids may be isolated directly from cells. Alternatively,the polymerase chain reaction (PCR) method can be used to produce thenucleic acids of the invention, using either chemically synthesizedstrands or genomic material as templates. Primers used for PCR can besynthesized using the sequence information provided herein and canfurther be designed to introduce appropriate new restriction sites, ifdesirable, to facilitate incorporation into a given vector forrecombinant expression.

The nucleic acids of the present invention may be flanked by natural S.pneumoniae regulatory sequences, or may be associated with heterologoussequences, including promoters, enhancers, response elements, signalsequences, polyadenylation sequences, introns, 5′- and 3′-noncodingregions, and the like. The nucleic acids may also be modified by manymeans known in the art. Non-limiting examples of such modificationsinclude methylation, “caps”, substitution of one or more of thenaturally occurring nucleotides with an analog, internucleotidemodifications such as, for example, those with uncharged linkages (e.g.,methyl phosphonates, phosphotriesters, phosphoroamidates, carbamates,etc.) and with charged linkages (e.g., phosphorothioates,phosphorodithioates, etc.). Nucleic acids may contain one or moreadditional covalently linked moieties, such as, for example, proteins(e.g., nucleases, toxins, antibodies, signal peptides, poly-L-lysine,etc.), intercalators (e.g., acridine, psoralen, etc.), chelators (e.g.,metals, radioactive metals, iron, oxidative metals, etc.), andalkylators. PNAs are also included. The nucleic acid may be derivatizedby formation of a methyl or ethyl phosphotriester or an alkylphosphoramidate linkage. Furthermore, the nucleic acid sequences of thepresent invention may also be modified with a label capable of providinga detectable signal, either directly or indirectly. Exemplary labelsinclude radioisotopes, fluorescent molecules, biotin, and the like.

The invention also provides nucleic acid vectors comprising thedisclosed S. pneumoniae-derived sequences or derivatives or fragmentsthereof. A large number of vectors, including plasmid and fungalvectors, have been described for replication and/or expression in avariety of eukaryotic and prokaryotic hosts, and may be used for genetherapy as well as for simple cloning or protein expression.

The encoded S. pneumoniae polypeptides may be expressed by using manyknown vectors, such as pUC plasmids, pET plasmids (Novagen, Inc.,Madison, Wis.), or pRSET or pREP (Invitrogen, San Diego, Calif.), andmany appropriate host cells, using methods disclosed or cited herein orotherwise known to those skilled in the relevant art. The particularchoice of vector/host is not critical to the practice of the invention.

Recombinant cloning vectors will often include one or more replicationsystems for cloning or expression, one or more markers for selection inthe host, e.g. antibiotic resistance, and one or more expressioncassettes. The inserted S. pneumoniae coding sequences may besynthesized by standard methods, isolated from natural sources, orprepared as hybrids, etc. Ligation of the S. pneumoniae coding sequencesto transcriptional regulatory elements and/or to other amino acid codingsequences may be achieved by known methods. Suitable host cells may betransformed/transfected/infected as appropriate by any suitable methodincluding electroporation, CaCl₂ mediated DNA uptake, fungal infection,microinjection, microprojectile, or other established methods.

Appropriate host cells include bacteria, archebacteria, fungi,especially yeast, and plant and animal cells, especially mammaliancells. Of particular interest are S. pneumoniae, E. coli, B. Subtilis,Saccharomyces cerevisiae, Saccharomyces carlsbergensis,Schizosaccharomyces pombi, SF9 cells, C129 cells, 293 cells, Neurospora,and CHO cells, COS cells, HeLa cells, and immortalized mammalian myeloidand lymphoid cell lines. Preferred replication systems include M13,ColE1, SV40, baculovirus, lambda, adenovirus, and the like. A largenumber of transcription initiation and termination regulatory regionshave been isolated and shown to be effective in the transcription andtranslation of heterologous proteins in the various hosts. Examples ofthese regions, methods of isolation, manner of manipulation, etc. areknown in the art. Under appropriate expression conditions, host cellscan be used as a source of recombinantly produced S. pneumoniae-derivedpeptides and polypeptides.

Advantageously, vectors may also include a transcription regulatoryelement (i.e., a promoter) operably linked to the S. pneumoniae portion.The promoter may optionally contain operator portions and/or ribosomebinding sites. Non-limiting examples of bacterial promoters compatiblewith E. coli include: b-lactamase (penicillinase) promoter; lactosepromoter; tryptophan (trp) promoter; araBAD (arabinose) operon promoter;lambda-derived P₁ promoter and N gene ribosome binding site; and thehybrid tac promoter derived from sequences of the trp and lac UV5promoters. Non-limiting examples of yeast promoters include3-phosphoglycerate kinase promoter, glyceraldehyde-3-phosphatedehydrogenase (GAPDH) promoter, galactokinase (GAL1) promoter,galactoepimerase promoter, and alcohol dehydrogenase (ADH) promoter.Suitable promoters for mammalian cells include without limitation viralpromoters such as that from Simian Virus 40 (SV40), Rous sarcoma virus(RSV), adenovirus (ADV), and bovine papilloma virus (BPV). Mammaliancells may also require terminator sequences, polyA addition sequencesand enhancer sequences to increase expression. Sequences which causeamplification of the gene may also be desirable. Furthermore, sequencesthat facilitate secretion of the recombinant product from cells,including, but not limited to, bacteria, yeast, and animal cells, suchas secretory signal sequences and/or prohormone pro region sequences,may also be included. These sequences are well described in the art.

Nucleic acids encoding wild-type or variant S. pneumoniae-derivedpolypeptides may also be introduced into cells by recombination events.For example, such a sequence can be introduced into a cell, and therebyeffect homologous recombination at the site of an endogenous gene or asequence with substantial identity to the gene. Otherrecombination-based methods such as nonhomologous recombinations ordeletion of endogenous genes by homologous recombination may also beused.

The nucleic acids of the present invention find use as templates for therecombinant production of S. pneumoniae-derived peptides orpolypeptides.

Identification and Use of S. pneumoniae Nucleic Acid Sequences

The disclosed S. pneumoniae polypeptide and nucleic acid sequences, orother sequences that are contained within ORFs, including completeprotein-coding sequences, of which any of the disclosed S.pneumoniae-specific sequences forms a part, are useful as targetcomponents for diagnosis and/or treatment of S. pneumoniae-causedinfection

It will be understood that the sequence of an entire protein-codingsequence of which each disclosed nucleic acid sequence forms a part canbe isolated and identified based on each disclosed sequence. This can beachieved, for example, by using an isolated nucleic acid encoding thedisclosed sequence, or fragments thereof, to prime a sequencing reactionwith genomic S. pneumoniae DNA as template; this is followed bysequencing the amplified product. The isolated nucleic acid encoding thedisclosed sequence, or fragments thereof, can also be hybridized to S.pneumoniae genomic libraries to identify clones containing additionalcomplete segments of the protein-coding sequence of which the shortersequence forms a part. Then, the entire protein-coding sequence, orfragments thereof, or nucleic acids encoding all or part of thesequence, or sequence-conservative or function-conservative variantsthereof, may be employed in practicing the present invention.

Preferred sequences are those that are useful in diagnostic and/ortherapeutic applications. Diagnostic applications include withoutlimitation nucleic-acid-based and antibody-based methods for detectingbacterial infection. Therapeutic applications include without limitationvaccines, passive immunotherapy, and drug treatments directed againstgene products that are both unique to bacteria and essential for growthand/or replication of bacteria.

Identification of Nucleic Acids Encoding Vaccine Components and Targetsfor Agents Effective Against S. pneumoniae

The disclosed S. pneumoniae genome sequence includes segments thatdirect the synthesis of ribonucleic acids and polypeptides, as well asorigins of replication, promoters, other types of regulatory sequences,and intergenic nucleic acids. The invention encompasses nucleic acidsencoding immunogenic components of vaccines and targets for agentseffective against S. pneumoniae. Identification of said immunogeniccomponents involved in the determination of the function of thedisclosed sequences, which can be achieved using a variety ofapproaches. Non-limiting examples of these approaches are describedbriefly below.

Homology to Known Sequences

Computer-assisted comparison of the disclosed S. pneumoniae sequenceswith previously reported sequences present in publicly availabledatabases is useful for identifying functional S. pneumoniae nucleicacid and polypeptide sequences. It will be understood thatprotein-coding sequences, for example, may be compared as a whole, andthat a high degree of sequence homology between two proteins (such as,for example, >80-90%) at the amino acid level indicates that the twoproteins also possess some degree of functional homology, such as, forexample, among enzymes involved in metabolism, DNA synthesis, or cellwall synthesis, and proteins involved in transport, cell division, etc.In addition, many structural features of particular protein classes havebeen identified and correlate with specific consensus sequences, suchas, for example, binding domains for nucleotides, DNA, metal ions, andother small molecules; sites for covalent modifications such asphosphorylation, acylation, and the like; sites of protein:proteininteractions, etc. These consensus sequences may be quite short and thusmay represent only a fraction of the entire protein-coding sequence.Identification of such a feature in an S. pneumoniae sequence istherefore useful in determining the function of the encoded protein andidentifying useful targets of antibacterial drugs.

Of particular relevance to the present invention are structural featuresthat are common to secretory, transmembrane, and surface proteins,including secretion signal peptides and hydrophobic transmembranedomains. S. pneumoniae proteins identified as containing putative signalsequences and/or transmembrane domains are useful as immunogeniccomponents of vaccines.

Targets for therapeutic drugs according to the invention include, butare not limited to, polypeptides of the invention, whether unique to S.pneumoniae or not, that are essential for growth and/or viability of S.pneumoniae under at least one growth condition. Polypeptides essentialfor growth and/or viability can be determined by examining the effect ofdeleting and/or disrupting the genes, i.e., by so-called gene“knockout”. Alternatively, genetic footprinting can be used (Smith etal., 1995, Proc. Natl. Acad. Sci. USA 92:5479-6433; PublishedInternational Application WO 94/26933; U.S. Pat. No. 5,612,180). Stillother methods for assessing essentiality includes the ability to isolateconditional lethal mutations in the specific gene (e.g., temperaturesensitive mutations). Other useful targets for therapeutic drugs, whichinclude polypeptides that are not essential for growth or viability perse but lead to loss of viability of the cell, can be used to targettherapeutic agents to cells.

Strain-specific Sequences

Because of the evolutionary relationship between different S. pneumoniaestrains, it is believed that the presently disclosed S. pneumoniaesequences are useful for identifying, and/or discriminating between,previously known and new S. pneumoniae strains. It is believed thatother S. pneumoniae strains will exhibit at least 70% sequence homologywith the presently disclosed sequence. Systematic and routine analysesof DNA sequences derived from samples containing S. pneumoniae strains,and comparison with the present sequence allows for the identificationof sequences that can be used to discriminate between strains, as wellas those that are common to all S. pneumoniae strains. In oneembodiment, the invention provides nucleic acids, including probes, andpeptide and polypeptide sequences that discriminate between differentstrains of S. pneumoniae. Strain-specific components can also beidentified functionally by their ability to elicit or react withantibodies that selectively recognize one or more S. pneumoniae strains.

In another embodiment, the invention provides nucleic acids, includingprobes, and peptide and polypeptide sequences that are common to all S.pneumoniae strains but are not found in other bacterial species.

S. pneumoniae Polypeptides

This invention encompasses isolated S. pneumoniae polypeptides encodedby the disclosed S. pneumoniae genomic sequences, including thepolypeptides of the invention contained in the Sequence Listing.Polypeptides of the invention are preferably at least 5 amino acidresidues in length. Using the DNA sequence information provided herein,the amino acid sequences of the polypeptides encompassed by theinvention can be deduced using methods well-known in the art. It will beunderstood that the sequence of an entire nucleic acid encoding an S.pneumoniae polypeptide can be isolated and identified based on an ORFthat encodes only a fragment of the cognate protein-coding region. Thiscan be achieved, for example, by using the isolated nucleic acidencoding the ORF, or fragments thereof, to prime a polymerase chainreaction with genomic S. pneumoniae DNA as template; this is followed bysequencing the amplified product.

The polypeptides of the present invention, includingfunction-conservative variants of the disclosed ORFs, may be isolatedfrom wild-type or mutant S. pneumoniae cells, or from heterologousorganisms or cells (including, but not limited to, bacteria, fungi,insect, plant, and mammalian cells) including S. pneumoniae into which aS. pneumoniae-derived protein-coding sequence has been introduced andexpressed. Furthermore, the polypeptides may be part of recombinantfusion proteins.

S. pneumoniae polypeptides of the invention can be chemicallysynthesized using commercially automated procedures such as thosereferenced herein, including, without limitation, exclusive solid phasesynthesis, partial solid phase methods, fragment condensation orclassical solution synthesis. The polypeptides are preferably preparedby solid phase peptide synthesis as described by Merrifield, 1963, J.Am. Chem. Soc. 85:2149. The synthesis is carried out with amino acidsthat are protected at the alpha-amino terminus. Trifunctional aminoacids with labile side-chains are also protected with suitable groups toprevent undesired chemical reactions from occurring during the assemblyof the polypeptides. The alpha-amino protecting group is selectivelyremoved to allow subsequent reaction to take place at theamino-terminus. The conditions for the removal of the alpha-aminoprotecting group do not remove the side-chain protecting groups.

The alpha-amino protecting groups are those known to be useful in theart of stepwise polypeptide synthesis. Included are acyl type protectinggroups, e.g., formyl, trifluoroacetyl, acetyl, aromatic urethane typeprotecting groups, e.g., benzyloxycarbonyl (Cbz), substitutedbenzyloxycarbonyl and 9-fluorenylmethyloxycarbonyl (Fmoc), aliphaticurethane protecting groups, e.g., t-butyloxycarbonyl (Boc),isopropyloxycarbonyl, cyclohexyloxycarbonyl, and alkyl type protectinggroups, e.g., benzyl, triphenylmethyl. The preferred protecting group isBoc. The side-chain protecting groups for Tyr include tetrahydropyranyl,tert-butyl, trityl, benzyl, Cbz, 4-Br-Cbz and 2,6-dichlorobenzyl. Thepreferred side-chain protecting group for Tyr is 2,6-dichlorobenzyl. Theside-chain protecting groups for Asp include benzyl, 2,6-dichlorobenzyl,methyl, ethyl and cyclohexyl. The preferred side-chain protecting groupfor Asp is cyclohexyl. The side-chain protecting groups for Thr and Serinclude acetyl, benzoyl, trityl, tetrahydropyranyl, benzyl,2,6-dichlorobenzyl and Cbz. The preferred protecting group for Thr andSer is benzyl. The side-chain protecting groups for Arg include nitro,Tos, Cbz, adamantyloxycarbonyl and Boc. The preferred protecting groupfor Arg is Tos. The side-chain amino group of Lys may be protected withCbz, 2-Cl-Cbz, Tos or Boc. The 2-Cl-Cbz group is the preferredprotecting group for Lys.

The side-chain protecting groups selected must remain intact duringcoupling and not be removed during the deprotection of theamino-terminus protecting group or during coupling conditions. Theside-chain protecting groups must also be removable upon the completionof synthesis, using reaction conditions that will not alter the finishedpolypeptide.

Solid phase synthesis is usually carried out from the carboxy-terminusby coupling the alpha-amino protected (side-chain protected) amino acidto a suitable solid support. An ester linkage is formed when theattachment is made to a chloromethyl or hydroxymethyl resin, and theresulting polypeptide will have a free carboxyl group at the C-terminus.Alternatively, when a benzhydrylamine or p-methylbenzhydrylamine resinis used, an amide bond is formed and the resulting polypeptide will havea carboxamide group at the C-terminus. These resins are commerciallyavailable, and their preparation was described by Stewart et al., 1984,Solid Phase Peptide Synthesis (2nd Edition), Pierce Chemical Co.,Rockford, Ill.

The C-terminal amino acid, protected at the side chain if necessary andat the alpha-amino group, is coupled to the benzhydrylamine resin usingvarious activating agents including dicyclohexylcarbodiimide (DCC),N,N′-diisopropyl-carbodiimide and carbonyldiimidazole. Following theattachment to the resin support, the alpha-amino protecting group isremoved using trifluoroacetic acid (TFA) or HCl in dioxane at atemperature between 0 and 25° C. Dimethylsulfide is added to the TFAafter the introduction of methionine (Met) to suppress possibleS-alkylation. After removal of the alpha-amino protecting group, theremaining protected amino acids are coupled stepwise in the requiredorder to obtain the desired sequence.

Various activating agents can be used for the coupling reactionsincluding DCC, N,N′-diisopropyl-carbodiimide,benzotriazol-1-yl-oxy-tris-(dimethylamino)-phosphoniumhexa-fluorophosphate (BOP) and DCC-hydroxybenzotriazole (HOBt). Eachprotected amino acid is used in excess (>2.0 equivalents), and thecouplings are usually carried out in N-methylpyrrolidone (NMP) or inDMF, CH₂Cl₂ or mixtures thereof. The extent of completion of thecoupling reaction is monitored at each stage, e.g., by the ninhydrinreaction as described by Kaiser et al., 1970, Anal. Biochem. 34:595. Incases where incomplete coupling is found, the coupling reaction isrepeated. The coupling reactions can be performed automatically withcommercially available instruments.

After the entire assembly of the desired polypeptide, thepolypeptide-resin is cleaved with a reagent such as liquid HF for 1-2hours at 0° C., which cleaves the polypeptide from the resin and removesall side-chain protecting groups. A scavenger such as anisole is usuallyused with the liquid HF to prevent cations formed during the cleavagefrom alkylating the amino acid residues present in the polypeptide. Thepolypeptide-resin may be deprotected with TFA/dithioethane prior tocleavage if desired.

Side-chain to side-chain cyclization on the solid support requires theuse of an orthogonal protection scheme which enables selective cleavageof the side-chain functions of acidic amino acids (e.g., Asp) and thebasic amino acids (e.g., Lys). The 9-fluorenylmethyl (Fm) protectinggroup for the side-chain of Asp and the 9-fluorenylmethyloxycarbonyl(Fmoc) protecting group for the side-chain of Lys can be used for thispurpose. In these cases, the side-chain protecting groups of theBoc-protected polypeptide-resin are selectively removed with piperidinein DMF. Cyclization is achieved on the solid support using variousactivating agents including DCC, DCC/HOBt or BOP. The HF reaction iscarried out on the cyclized polypeptide-resin as described above.

Methods for polypeptide purification are well-known in the art,including, without limitation, preparative disc-gel electrophoresis,isoelectric focusing, HPLC, reversed-phase HPLC, gel filtration, ionexchange and partition chromatography, and countercurrent distribution.For some purposes, it is preferable to produce the polypeptide in arecombinant system in which the S. pneumoniae protein contains anadditional sequence tag that facilitates purification, such as, but notlimited to, a polyhistidine sequence. The polypeptide can then bepurified from a crude lysate of the host cell by chromatography on anappropriate solid-phase matrix. Alternatively, antibodies producedagainst a S. pneumoniae protein or against peptides derived therefromcan be used as purification reagents. Other purification methods arepossible.

The present invention also encompasses derivatives and homologues of S.pneumoniae-encoded polypeptides. For some purposes, nucleic acidsequences encoding the peptides may be altered by substitutions,additions, or deletions that provide for functionally equivalentmolecules, i.e., function-conservative variants. For example, one ormore amino acid residues within the sequence can be substituted byanother amino acid of similar properties, such as, for example,positively charged amino acids (arginine, lysine, and histidine);negatively charged amino acids (aspartate and glutamate); polar neutralamino acids; and non-polar amino acids. The isolated polypeptides may bemodified by, for example, phosphorylation, sulfation, acylation, orother protein modifications. They may also be modified with a labelcapable of providing a detectable signal, either directly or indirectly,including, but not limited to, radioisotopes and fluorescent compounds.

To identify S. pneumoniae-derived polypeptides for use in the presentinvention, essentially the complete genomic sequence of a virulent,methicillin-resistant isolate of Streptococcus pneumoniae isolate wasanalyzed. While, in very rare instances, a nucleic acid sequencing errormay be revealed, resolving a rare sequencing error is well within theart, and such an occurrence will not prevent one skilled in the art frompracticing the invention.

Also encompassed are any S. pneumoniae polypeptide sequences that arecontained within the open reading frames (ORFs), including completeprotein-coding sequences, of which any of SEQ ID NO: 2662-SEQ ID NO:5322 forms a part. Table 2, which is appended herewith and which formspart of the present specification, provides a putative identification ofthe particular function of a polypeptide which is encoded by each ORF.As a result, one skilled in the art can use the polypeptides of thepresent invention for commercial and industrial purposes consistent withthe type of putative identification of the polypeptide.

The present invention provides a library of S. Pneumoniae-derivedpolypeptide sequences, and a corresponding library of nucleic acidsequences encoding the polypeptides, wherein the polypeptidesthemselves, or polypeptides contained within ORFs of which they form apart, comprise sequences that are contemplated for use as components ofvaccines. Non-limiting examples of such sequences are listed by SEQ IDNO in Table 2, which is appended herewith and which forms part of thepresent specification.

The present invention also provides a library of S. pneumoniae-derivedpolypeptide sequences, and a corresponding library of nucleic acidsequences encoding the polypeptides, wherein the polypeptidesthemselves, or polypeptides contained within ORFs of which they form apart, comprise sequences lacking homology to any known prokaryotic oreukaryotic sequences. Such libraries provide probes, primers, andmarkers which can be used to diagnose S. pneumoniae infection, includinguse as markers in epidemiological studies. Non-limiting examples of suchsequences are listed by SEQ ID NO in Table 2, which is appended

The present invention also provides a library of S. pneumoniae-derivedpolypeptide sequences, and a corresponding library of nucleic acidsequences encoding the polypeptides, wherein the polypeptidesthemselves, or polypeptides contained within ORFs of which they form apart, comprise targets for therapeutic drugs.

Specific Example Determination of Candidate Protein Antigens forAntibody and Vaccine Development

The selection of candidate protein antigens for vaccine development canbe derived from the nucleic acids encoding S. pneumoniae polypeptides.First, the ORF's can be analyzed for homology to other known exported ormembrane proteins and analyzed using the discriminant analysis describedby Klein, et al. (Klein, P., Kanehsia, M., and DeLisi, C. (1985)Biochimica et Biophysica Acta 815, 468-476) for predicting exported andmembrane proteins.

Homology searches can be performed using the BLAST algorithm containedin the Wisconsin Sequence Analysis Package (Genetics Computer Group,University Research Park, 575 Science Drive, Madison, Wis. 53711) tocompare each predicted ORF amino acid sequence with all sequences foundin the current GenBank, SWISS-PROT and PIR databases. BLAST searches forlocal alignments between the ORF and the databank sequences and reportsa probability score which indicates the probability of finding thissequence by chance in the database. ORF's with significant homology(e.g. probabilities lower than 1×10⁻⁶ that the homology is only due torandom chance) to membrane or exported proteins represent proteinantigens for vaccine development. Possible functions can be provided toS. pneumoniae genes based on sequence homology to genes cloned in otherorganisms.

Discriminant analysis (Klein, et al. supra) can be used to examine theORF amino acid sequences. This algorithm uses the intrinsic informationcontained in the ORF amino acid sequence and compares it to informationderived from the properties of known membrane and exported proteins.This comparison predicts which proteins will be exported, membraneassociated or cytoplasmic. ORF amino acid sequences identified asexported or membrane associated by this algorithm are likely proteinantigens for vaccine development.

Production of Fragments and Analogs of S. pneumoniae Nucleic Acids andPolypeptides

Based on the discovery of the S. pneumoniae gene products of theinvention provided in the Sequence Listing, one skilled in the art canalter the disclosed structure (of S. pneumoniae genes), e.g., byproducing fragments or analogs, and test the newly produced structuresfor activity. Examples of techniques known to those skilled in therelevant art which allow the production and testing of fragments andanalogs are discussed below. These, or analogous methods can be used tomake and screen libraries of polypeptides, e.g., libraries of randompeptides or libraries of fragments or analogs of cellular proteins forthe ability to bind S. pneumoniae polypeptides. Such screens are usefulfor the identification of inhibitors of S. pneumoniae.

Generation of Fragments

Fragments of a protein can be produced in several ways, e.g.,recombinantly, by proteolytic digestion, or by chemical synthesis.Internal or terminal fragments of a polypeptide can be generated byremoving one or more nucleotides from one end (for a terminal fragment)or both ends (for an internal fragment) of a nucleic acid which encodesthe polypeptide. Expression of the mutagenized DNA produces polypeptidefragments. Digestion with “end-nibbling” endonucleases can thus generateDNA's which encode an array of fragments. DNA's which encode fragmentsof a protein can also be generated by random shearing, restrictiondigestion or a combination of the above-discussed methods.

Fragments can also be chemically synthesized using techniques known inthe art such as conventional Merrifield solid phase f-Moc or t-Bocchemistry. For example, peptides of the present invention may bearbitrarily divided into fragments of desired length with no overlap ofthe fragments, or divided into overlapping fragments of a desiredlength.

Alteration of Nucleic Acids and Polypeptides: Random Methods

Amino acid sequence variants of a protein can be prepared by randommutagenesis of DNA which encodes a protein or a particular domain orregion of a protein. Useful methods include PCR mutagenesis andsaturation mutagenesis. A library of random amino acid sequence variantscan also be generated by the synthesis of a set of degenerateoligonucleotide sequences. (Methods for screening proteins in a libraryof variants are elsewhere herein).

PCR Mutagenesis

In PCR mutagenesis, reduced Taq polymerase fidelity is used to introducerandom mutations into a cloned fragment of DNA (Leung et al., 1989,Technique 1:11-15). The DNA region to be mutagenized is amplified usingthe polymerase chain reaction (PCR) under conditions that reduce thefidelity of DNA synthesis by Taq DNA polymerase, e.g., by using adGTP/dATP ratio of five and adding Mn²⁺ to the PCR reaction. The pool ofamplified DNA fragments are inserted into appropriate cloning vectors toprovide random mutant libraries.

Saturation Mutagenesis

Saturation mutagenesis allows for the rapid introduction of a largenumber of single base substitutions into cloned DNA fragments (Mayers etal., 1985, Science 229:242). This technique includes generation ofmutations, e.g., by chemical treatment or irradiation of single-strandedDNA in vitro, and synthesis of a complimentary DNA strand. The mutationfrequency can be modulated by modulating the severity of the treatment,and essentially all possible base substitutions can be obtained. Becausethis procedure does not involve a genetic selection for mutant fragmentsboth neutral substitutions, as well as those that alter function, areobtained. The distribution of point mutations is not biased towardconserved sequence elements.

Degenerate Oligonucleotides

A library of homologs can also be generated from a set of degenerateoligonucleotide sequences. Chemical synthesis of a degenerate sequencescan be carried out in an automatic DNA synthesizer, and the syntheticgenes then ligated into an appropriate expression vector. The synthesisof degenerate oligonucleotides is known in the art (see for example,Narang, S A (1983) Tetrahedron 39:3; Itakura et al. (1981) RecombinantDNA, Proc 3rd Cleveland Sympos. Macromolecules, ed. A G Walton,Amsterdam: Elsevier pp 273-289; Itakura et al. (1984) Annu. Rev.Biochem. 53:323; Itakura et al. (1984) Science 198:1056; Ike et al.(1983) Nucleic Acid Res. 11:477. Such techniques have been employed inthe directed evolution of other proteins (see, for example, Scott et al.(1990) Science 249:386-390; Roberts et al. (1992) PNAS 89:2429-2433;Devlin et al. (1990) Science 249: 404-406; Cwirla et al. (1990) PNAS 87:6378-6382; as well as U.S. Pat. Nos. 5,223,409, 5,198,346, and5,096,815).

Alteration of Nucleic Acids and Polypeptides: Methods for DirectedMutagenesis

Non-random or directed, mutagenesis techniques can be used to providespecific sequences or mutations in specific regions. These techniquescan be used to create variants which include, e.g., deletions,insertions, or substitutions, of residues of the known amino acidsequence of a protein. The sites for mutation can be modifiedindividually or in series, e.g., by (1) substituting first withconserved amino acids and then with more radical choices depending uponresults achieved, (2) deleting the target residue, or (3) insertingresidues of the same or a different class adjacent to the located site,or combinations of options 1-3.

Alanine Scanning Mutagenesis

Alanine scanning mutagenesis is a useful method for identification ofcertain residues or regions of the desired protein that are preferredlocations or domains for mutagenesis, Cunningham and Wells (Science244:1081-1085, 1989). In alanine scanning, a residue or group of targetresidues are identified (e.g., charged residues such as Arg, Asp, His,Lys, and Glu) and replaced by a neutral or negatively charged amino acid(most preferably alanine or polyalanine). Replacement of an amino acidcan affect the interaction of the amino acids with the surroundingaqueous environment in or outside the cell. Those domains demonstratingfunctional sensitivity to the substitutions are then refined byintroducing further or other variants at or for the sites ofsubstitution. Thus, while the site for introducing an amino acidsequence variation is predetermined, the nature of the mutation per seneed not be predetermined. For example, to optimize the performance of amutation at a given site, alanine scanning or random mutagenesis may beconducted at the target codon or region and the expressed desiredprotein subunit variants are screened for the optimal combination ofdesired activity.

Oligonucleotide-Mediated Mutagenesis

Oligonucleotide-mediated mutagenesis is a useful method for preparingsubstitution, deletion, and insertion variants of DNA, see, e.g.,Adelman et al., (DNA 2:183, 1983). Briefly, the desired DNA is alteredby hybridizing an oligonucleotide encoding a mutation to a DNA template,where the template is the single-stranded form of a plasmid orbacteriophage containing the unaltered or native DNA sequence of thedesired protein. After hybridization, a DNA polymerase is used tosynthesize an entire second complementary strand of the template thatwill thus incorporate the oligonucleotide primer, and will code for theselected alteration in the desired protein DNA. Generally,oligonucleotides of at least 25 nucleotides in length are used. Anoptimal oligonucleotide will have 12 to 15 nucleotides that arecompletely complementary to the template on either side of thenucleotide(s) coding for the mutation. This ensures that theoligonucleotide will hybridize properly to the single-stranded DNAtemplate molecule. The oligonucleotides are readily synthesized usingtechniques known in the art such as that described by Crea et al. (Proc.Natl. Acad. Sci. USA, 75: 5765[1978]).

Cassette Mutagenesis

Another method for preparing variants, cassette mutagenesis, is based onthe technique described by Wells et al. (Gene, 34:315[1985]). Thestarting material is a plasmid (or other vector) which includes theprotein subunit DNA to be mutated. The codon(s) in the protein subunitDNA to be mutated are identified. There must be a unique restrictionendonuclease site on each side of the identified mutation site(s). If nosuch restriction sites exist, they may be generated using theabove-described oligonucleotide-mediated mutagenesis method to introducethem at appropriate locations in the desired protein subunit DNA. Afterthe restriction sites have been introduced into the plasmid, the plasmidis cut at these sites to linearize it. A double-stranded oligonucleotideencoding the sequence of the DNA between the restriction sites butcontaining the desired mutation(s) is synthesized using standardprocedures. The two strands are synthesized separately and thenhybridized together using standard techniques. This double-strandedoligonucleotide is referred to as the cassette. This cassette isdesigned to have 3′ and 5′ ends that are comparable with the ends of thelinearized plasmid, such that it can be directly ligated to the plasmid.This plasmid now contains the mutated desired protein subunit DNAsequence.

Combinatorial Mutagenesis

Combinatorial mutagenesis can also be used to generate mutants (Ladneret al., WO 88/06630). In this method, the amino acid sequences for agroup of homologs or other related proteins are aligned, preferably topromote the highest homology possible. All of the amino acids whichappear at a given position of the aligned sequences can be selected tocreate a degenerate set of combinatorial sequences. The variegatedlibrary of variants is generated by combinatorial mutagenesis at thenucleic acid level, and is encoded by a variegated gene library. Forexample, a mixture of synthetic oligonucleotides can be enzymaticallyligated into gene sequences such that the degenerate set of potentialsequences are expressible as individual peptides, or alternatively, as aset of larger fusion proteins containing the set of degeneratesequences.

Other Modifications of S. pneumoniae Nucleic Acids and Polypeptides

It is possible to modify the structure of an S. pneumoniae polypeptidefor such purposes as increasing solubility, enhancing stability (e.g.,shelf life ex vivo and resistance to proteolytic degradation in vivo). Amodified S. pneumoniae protein or peptide can be produced in which theamino acid sequence has been altered, such as by amino acidsubstitution, deletion, or addition as described herein.

An S. pneumoniae peptide can also be modified by substitution ofcysteine residues preferably with alanine, serine, threonine, leucine orglutamic acid residues to minimize dimerization via disulfide linkages.In addition, amino acid side chains of fragments of the protein of theinvention can be chemically modified. Another modification iscyclization of the peptide.

In order to enhance stability and/or reactivity, an S. pneumoniaepolypeptide can be modified to incorporate one or more polymorphisms inthe amino acid sequence of the protein resulting from any naturalallelic variation. Additionally, D-amino acids, non-natural amino acids,or non-amino acid analogs can be substituted or added to produce amodified protein within the scope of this invention. Furthermore, an S.pneumoniae polypeptide can be modified using polyethylene glycol (PEG)according to the method of A. Sehon and co-workers (Wie et al., supra)to produce a protein conjugated with PEG. In addition, PEG can be addedduring chemical synthesis of the protein. Other modifications of S.pneumoniae proteins include reduction/alkylation (Tarr, Methods ofProtein Microcharacterization, J. E. Silver ed., Humana Press, CliftonN.J. 155-194 (1986)); acylation (Tarr, supra); chemical coupling to anappropriate carrier (Mishell and Shiigi, eds, Selected Methods inCellular Immunology, WH Freeman, San Francisco, Calif. (1980), U.S. Pat.No. 4,939,239; or mild formalin treatment (Marsh, (1971) Int. Arch. ofAllergy and Appl. Immunol., 41: 199-215).

To facilitate purification and potentially increase solubility of an S.pneumoniae protein or peptide, it is possible to add an amino acidfusion moiety to the peptide backbone. For example, hexa-histidine canbe added to the protein for purification by immobilized metal ionaffinity chromatography (Hochuli, E. et al., (1988) Bio/Technology, 6:1321-1325). In addition, to facilitate isolation of peptides free ofirrelevant sequences, specific endoprotease cleavage sites can beintroduced between the sequences of the fusion moiety and the peptide.

To potentially aid proper antigen processing of epitopes within an S.pneumoniae polypeptide, canonical protease sensitive sites can beengineered between regions, each comprising at least one epitope viarecombinant or synthetic methods. For example, charged amino acid pairs,such as KK or RR, can be introduced between regions within a protein orfragment during recombinant construction thereof. The resulting peptidecan be rendered sensitive to cleavage by cathepsin and/or othertrypsin-like enzymes which would generate portions of the proteincontaining one or more epitopes. In addition, such charged amino acidresidues can result in an increase in the solubility of the peptide.

Primary Methods for Screening Polypeptides and Analogs

Various techniques are known in the art for screening generated mutantgene products. Techniques for screening large gene libraries ofteninclude cloning the gene library into replicable expression vectors,transforming appropriate cells with the resulting library of vectors,and expressing the genes under conditions in which detection of adesired activity, e.g., in this case, binding to S. pneumoniaepolypeptide or an interacting protein, facilitates relatively easyisolation of the vector encoding the gene whose product was detected.Each of the techniques described below is amenable to high through-putanalysis for screening large numbers of sequences created, e.g., byrandom mutagenesis techniques.

Two Hybrid Systems

Two hybrid assays such as the system described above (as with the otherscreening methods described herein), can be used to identifypolypeptides, e.g., fragments or analogs of a naturally-occurring S.pneumoniae polypeptide, e.g., of cellular proteins, or of randomlygenerated polypeptides which bind to an S. pneumoniae protein. (The S.pneumoniae domain is used as the bait protein and the library ofvariants are expressed as prey fusion proteins.) In an analogousfashion, a two hybrid assay (as with the other screening methodsdescribed herein), can be used to find polypeptides which bind a S.pneumoniae polypeptide.

Display Libraries

In one approach to screening assays, the candidate peptides aredisplayed on the surface of a cell or viral particle, and the ability ofparticular cells or viral particles to bind an appropriate receptorprotein via the displayed product is detected in a “panning assay”. Forexample, the gene library can be cloned into the gene for a surfacemembrane protein of a bacterial cell, and the resulting fusion proteindetected by panning (Ladner et al., WO 88/06630; Fuchs et al. (1991)Bio/Technology 9:1370-1371; and Goward et al. (1992) TIBS 18:136-140).In a similar fashion, a detectably labeled ligand can be used to scorefor potentially functional peptide homologs. Fluorescently labeledligands, e.g., receptors, can be used to detect homologs which retainligand-binding activity. The use of fluorescently labeled ligands,allows cells to be visually inspected and separated under a fluorescencemicroscope, or, where the morphology of the cell permits, to beseparated by a fluorescence-activated cell sorter.

A gene library can be expressed as a fusion protein on the surface of aviral particle. For instance, in the filamentous phage system, foreignpeptide sequences can be expressed on the surface of infectious phage,thereby conferring two significant benefits. First, since these phagecan be applied to affinity matrices at concentrations well over 10¹³phage per milliliter, a large number of phage can be screened at onetime. Second, since each infectious phage displays a gene product on itssurface, if a particular phage is recovered from an affinity matrix inlow yield, the phage can be amplified by another round of infection. Thegroup of almost identical E. coli filamentous phages M13, fd., and flare most often used in phage display libraries. Either of the phage gIIIor gVIII coat proteins can be used to generate fusion proteins withoutdisrupting the ultimate packaging of the viral particle. Foreignepitopes can be expressed at the NH₂-terminal end of pIII and phagebearing such epitopes recovered from a large excess of phage lackingthis epitope (Ladner et al. PCT publication WO 90/02909; Garrard et al.,PCT publication WO 92/09690; Marks et al. (1992) J. Biol. Chem.267:16007-16010; Griffiths et al. (1993) EMBO J. 12:725-734; Clackson etal. (1991) Nature 352:624-628; and Barbas et al. (1992) PNAS89:4457-4461).

A common approach uses the maltose receptor of E. coli (the outermembrane protein, LamB) as a peptide fusion partner (Charbit et al.(1986) EMBO 5, 3029-3037). Oligonucleotides have been inserted intoplasmids encoding the LamB gene to produce peptides fused into one ofthe extracellular loops of the protein. These peptides are available forbinding to ligands, e.g., to antibodies, and can elicit an immuneresponse when the cells are administered to animals. Other cell surfaceproteins, e.g., OmpA (Schorr et al. (1991) Vaccines 91, pp. 387-392),PhoE (Agterberg, et al. (1990) Gene 88, 37-45), and PAL (Fuchs et al.(1991) Bio/Tech 9, 1369-1372), as well as large bacterial surfacestructures have served as vehicles for peptide display. Peptides can befused to pilin, a protein which polymerizes to form the pilus-a conduitfor interbacterial exchange of genetic information (Thiry et al. (1989)Appl. Environ. Microbiol. 55, 984-993). Because of its role ininteracting with other cells, the pilus provides a useful support forthe presentation of peptides to the extracellular environment. Anotherlarge surface structure used for peptide display is the bacterial motiveorgan, the flagellum. Fusion of peptides to the subunit proteinflagellin offers a dense array of many peptide copies on the host cells(Kuwajima et al. (1988) Bio/Tech. 6, 1080-1083). Surface proteins ofother bacterial species have also served as peptide fusion partners.Examples include the Staphylococcus protein A and the outer membrane IgAprotease of Neisseria (Hansson et al. (1992) J. Bacteriol. 174,4239-4245 and Klauser et al. (1990) EMBO J. 9, 1991-1999).

In the filamentous phage systems and the LamB system described above,the physical link between the peptide and its encoding DNA occurs by thecontainment of the DNA within a particle (cell or phage) that carriesthe peptide on its surface. Capturing the peptide captures the particleand the DNA within. An alternative scheme uses the DNA-binding proteinLacI to form a link between peptide and DNA (Cull et al. (1992) PNAS USA89:1865-1869). This system uses a plasmid containing the LacI gene withan oligonucleotide cloning site at its 3′-end. Under the controlledinduction by arabinose, a LacI-peptide fusion protein is produced. Thisfusion retains the natural ability of LacI to bind to a short DNAsequence known as LacO operator (LacO). By installing two copies of LacOon the expression plasmid, the LacI-peptide fusion binds tightly to theplasmid that encoded it. Because the plasmids in each cell contain onlya single oligonucleotide sequence and each cell expresses only a singlepeptide sequence, the peptides become specifically and stablelyassociated with the DNA sequence that directed its synthesis. The cellsof the library are gently lysed and the peptide-DNA complexes areexposed to a matrix of immobilized receptor to recover the complexescontaining active peptides. The associated plasmid DNA is thenreintroduced into cells for amplification and DNA sequencing todetermine the identity of the peptide ligands. As a demonstration of thepractical utility of the method, a large random library ofdodecapeptides was made and selected on a monoclonal antibody raisedagainst the opioid peptide dynorphin B. A cohort of peptides wasrecovered, all related by a consensus sequence corresponding to asix-residue portion of dynorphin B. (Cull et al. (1992) Proc. Natl.Acad. Sci. U.S.A. 89-1869)

This scheme, sometimes referred to as peptides-on-plasmids, differs intwo important ways from the phage display methods. First, the peptidesare attached to the C-terminus of the fusion protein, resulting in thedisplay of the library members as peptides having free carboxy termini.Both of the filamentous phage coat proteins, pill and pVIII, areanchored to the phage through their C-termini, and the guest peptidesare placed into the outward-extending N-terminal domains. In somedesigns, the phage-displayed peptides are presented right at the aminoterminus of the fusion protein. (Cwirla, et al. (1990) Proc. Natl. Acad.Sci. U.S.A. 87, 6378-6382) A second difference is the set of biologicalbiases affecting the population of peptides actually present in thelibraries. The LacI fusion molecules are confined to the cytoplasm ofthe host cells. The phage coat fusions are exposed briefly to thecytoplasm during translation but are rapidly secreted through the innermembrane into the periplasmic compartment, remaining anchored in themembrane by their C-terminal hydrophobic domains, with the N-termini,containing the peptides, protruding into the periplasm while awaitingassembly into phage particles. The peptides in the LacI and phagelibraries may differ significantly as a result of their exposure todifferent proteolytic activities. The phage coat proteins requiretransport across the inner membrane and signal peptidase processing as aprelude to incorporation into phage. Certain peptides exert adeleterious effect on these processes and are underrepresented in thelibraries (Gallop et al. (1994) J. Med. Chem. 37(9):1233-1251). Theseparticular biases are not a factor in the LacI display system.

The number of small peptides available in recombinant random librariesis enormous. Libraries of 10⁷-10⁹ independent clones are routinelyprepared. Libraries as large as 10¹¹ recombinants have been created, butthis size approaches the practical limit for clone libraries. Thislimitation in library size occurs at the step of transforming the DNAcontaining randomized segments into the host bacterial cells. Tocircumvent this limitation, an in vitro system based on the display ofnascent peptides in polysome complexes has recently been developed. Thisdisplay library method has the potential of producing libraries 3-6orders of magnitude larger than the currently available phage/phagemidor plasmid libraries. Furthermore, the construction of the libraries,expression of the peptides, and screening, is done in an entirelycell-free format.

In one application of this method (Gallop et al. (1994) J. Med. Chem.37(9):1233-1251), a molecular DNA library encoding 10¹² decapeptides wasconstructed and the library expressed in an E. coli S30 in vitro coupledtranscription/translation system. Conditions were chosen to stall theribosomes on the mRNA, causing the accumulation of a substantialproportion of the RNA in polysomes and yielding complexes containingnascent peptides still linked to their encoding RNA. The polysomes aresufficiently robust to be affinity purified on immobilized receptors inmuch the same way as the more conventional recombinant peptide displaylibraries are screened. RNA from the bound complexes is recovered,converted to cDNA, and amplified by PCR to produce a template for thenext round of synthesis and screening. The polysome display method canbe coupled to the phage display system. Following several rounds ofscreening, cDNA from the enriched pool of polysomes was cloned into aphagemid vector. This vector serves as both a peptide expression vector,displaying peptides fused to the coat proteins, and as a DNA sequencingvector for peptide identification. By expressing the polysome-derivedpeptides on phage, one can either continue the affinity selectionprocedure in this format or assay the peptides on individual clones forbinding activity in a phage ELISA, or for binding specificity in acompletion phage ELISA (Barret, et al. (1992) Anal. Biochem 204,357-364). To identify the sequences of the active peptides one sequencesthe DNA produced by the phagemid host.

Secondary Screening of Polypeptides and Analogs

The high through-put assays described above can be followed by secondaryscreens in order to identify further biological activities which will,e.g., allow one skilled in the art to differentiate agonists fromantagonists. The type of a secondary screen used will depend on thedesired activity that needs to be tested. For example, an assay can bedeveloped in which the ability to inhibit an interaction between aprotein of interest and its respective ligand can be used to identifyantagonists from a group of peptide fragments isolated though one of theprimary screens described above.

Therefore, methods for generating fragments and analogs and testing themfor activity are known in the art. Once the core sequence of interest isidentified, it is routine for one skilled in the art to obtain analogsand fragments.

Peptide Mimetics of S. pneumoniae Polypeptides

The invention also provides for reduction of the protein binding domainsof the subject S. pneumoniae polypeptides to generate mimetics, e.g.peptide or non-peptide agents. The peptide mimetics are able to disruptbinding of a polypeptide to its counter ligand, e.g., in the case of anS. pneumoniae polypeptide binding to a naturally occurring ligand. Thecritical residues of a subject S. pneumoniae polypeptide which areinvolved in molecular recognition of a polypeptide can be determined andused to generate S. pneumoniae-derived peptidomimetics whichcompetitively or noncompetitively inhibit binding of the S. pneumoniaepolypeptide with an interacting polypeptide (see, for example, Europeanpatent applications EP-412,762A and EP-B31,080A).

For example, scanning mutagenesis can be used to map the amino acidresidues of a particular S. pneumoniae polypeptide involved in bindingan interacting polypeptide, peptidomimetic compounds (e.g. diazepine orisoquinoline derivatives) can be generated which mimic those residues inbinding to an interacting polypeptide, and which therefore can inhibitbinding of an S. pneumoniae polypeptide to an interacting polypeptideand thereby interfere with the function of S. pneumoniae polypeptide.For instance, non-hydrolyzable peptide analogs of such residues can begenerated using benzodiazepine (e.g., see Freidinger et al. in Peptides:Chemistry and Biology, G. R. Marshall ed., ESCOM Publisher: Leiden,Netherlands, 1988), azepine (e.g., see Huffinan et al. in Peptides:Chemistry and Biology, G. R. Marshall ed., ESCOM Publisher: Leiden,Netherlands, 1988), substituted gama lactam rings (Garvey et al. inPeptides: Chemistry and Biology, G. R. Marshall ed., ESCOM Publisher:Leiden, Netherlands, 1988), keto-methylene pseudopeptides (Ewenson etal. (1986) J Med Chem 29:295; and Ewenson et al. in Peptides: Structureand Function (Proceedings of the 9th American Peptide Symposium) PierceChemical Co. Rockland, Ill., 1985), b-turn dipeptide cores (Nagai et al.(1985) Tetrahedron Lett 26:647; and Sato et al. (1986) J Chem Soc PerkinTrans 1:1231), and b-aminoalcohols (Gordon et al. (1985) Biochem BiophysRes Commun 126:419; and et al. (1986) Biochem Biophys Res Commun134:71).

Vaccine Formulations for S. pneumoniae Nucleic Acids and Polypeptides

This invention also features vaccine compositions for protection againstinfection by S. pneumoniae or for treatment of S. pneumoniae infection,a gram-negative spiral microaerophilic bacterium. In one embodiment, thevaccine compositions contain one or more immunogenic components such asa surface protein from S. pneumoniae, or portion thereof, and apharmaceutically acceptable carrier. Nucleic acids within the scope ofthe invention are exemplified by the nucleic acids of the inventioncontained in the Sequence Listing which encode S. pneumoniae surfaceproteins. Any nucleic acid encoding an immunogenic S. pneumoniaeprotein, or portion thereof, which is capable of expression in a cell,can be used in the present invention. These vaccines have therapeuticand prophylactic utilities.

One aspect of the invention provides a vaccine composition forprotection against infection by S. pneumoniae which contains at leastone immunogenic fragment of an S. pneumoniae protein and apharmaceutically acceptable carrier. Preferred fragments includepeptides of at least about 10 amino acid residues in length, preferablyabout 10-20 amino acid residues in length, and more preferably about12-16 amino acid residues in length.

Immunogenic components of the invention can be obtained, for example, byscreening polypeptides recombinantly produced from the correspondingfragment of the nucleic acid encoding the full-length S. pneumoniaeprotein. In addition, fragments can be chemically synthesized usingtechniques known in the art such as conventional Merrifield solid phasef-Moc or t-Boc chemistry.

In one embodiment, immunogenic components are identified by the abilityof the peptide to stimulate T cells. Peptides which stimulate T cells,as determined by, for example, T cell proliferation or cytokinesecretion are defined herein as comprising at least one T cell epitope.T cell epitopes are believed to be involved in initiation andperpetuation of the immune response to the protein allergen which isresponsible for the clinical symptoms of allergy. These T cell epitopesare thought to trigger early events at the level of the T helper cell bybinding to an appropriate HLA molecule on the surface of an antigenpresenting cell, thereby stimulating the T cell subpopulation with therelevant T cell receptor for the epitope. These events lead to T cellproliferation, lymphokine secretion, local inflammatory reactions,recruitment of additional immune cells to the site of antigen/T cellinteraction, and activation of the B cell cascade, leading to theproduction of antibodies. A T cell epitope is the basic element, orsmallest unit of recognition by a T cell receptor, where the epitopecomprises amino acids essential to receptor recognition (e.g.,approximately 6 or 7 amino acid residues). Amino acid sequences whichmimic those of the T cell epitopes are within the scope of thisinvention.

Screening immunogenic components can be accomplished using one or moreof several different assays. For example, in vitro, peptide T cellstimulatory activity is assayed by contacting a peptide known orsuspected of being immunogenic with an antigen presenting cell whichpresents appropriate MHC molecules in a T cell culture. Presentation ofan immunogenic S. pneumoniae peptide in association with appropriate MHCmolecules to T cells in conjunction with the necessary co-stimulationhas the effect of transmitting a signal to the T cell that induces theproduction of increased levels of cytokines, particularly ofinterleukin-2 and interleukin-4. The culture supernatant can be obtainedand assayed for interleukin-2 or other known cytokines. For example, anyone of several conventional assays for interleukin-2 can be employed,such as the assay described in Proc. Natl. Acad. Sci USA, 86: 1333(1989) the pertinent portions of which are incorporated herein byreference. A kit for an assay for the production of interferon is alsoavailable from Genzyme Corporation (Cambridge, Mass.).

Alternatively, a common assay for T cell proliferation entails measuringtritiated thymidine incorporation. The proliferation of T cells can bemeasured in vitro by determining the amount of ³H-labeled thymidineincorporated into the replicating DNA of cultured cells. Therefore, therate of DNA synthesis and, in turn, the rate of cell division can bequantified.

Vaccine compositions of the invention containing immunogenic components(e.g., S. pneumoniae polypeptide or fragment thereof or nucleic acidencoding an S. pneumoniae polypeptide or fragment thereof) preferablyinclude a pharmaceutically acceptable carrier. The term“pharmaceutically acceptable carrier” refers to a carrier that does notcause an allergic reaction or other untoward effect in patients to whomit is administered. Suitable pharmaceutically acceptable carriersinclude, for example, one or more of water, saline, phosphate bufferedsaline, dextrose, glycerol, ethanol and the like, as well ascombinations thereof. Pharmaceutically acceptable carriers may furthercomprise minor amounts of auxiliary substances such as wetting oremulsifying agents, preservatives or buffers, which enhance the shelflife or effectiveness of the antibody. For vaccines of the inventioncontaining S. pneumoniae polypeptides, the polypeptide isco-administered with a suitable adjuvant.

It will be apparent to those of skill in the art that thetherapeutically effective amount of DNA or protein of this inventionwill depend, inter alia, upon the administration schedule, the unit doseof antibody administered, whether the protein or DNA is administered incombination with other therapeutic agents, the immune status and healthof the patient, and the therapeutic activity of the particular proteinor DNA.

Vaccine compositions are conventionally administered parenterally, e.g.,by injection, either subcutaneously or intramuscularly. Methods forintramuscular immunization are described by Wolff et al. (1990) Science247: 1465-1468 and by Sedegah et al. (1994) Immunology 91: 9866-9870.Other modes of administration include oral and pulmonary formulations,suppositories, and transdermal applications. Oral immunization ispreferred over parenteral methods for inducing protection againstinfection by S. pneumoniae. Cain et. al. (1993) Vaccine 11: 637-642.Oral formulations include such normally employed excipients as, forexample, pharmaceutical grades of mannitol, lactose, starch, magnesiumstearate, sodium saccharine, cellulose, magnesium carbonate, and thelike.

The vaccine compositions of the invention can include an adjuvant,including, but not limited to aluminum hydroxide;N-acetyl-muramyl-L-threonyl-D-isoglutamine (thr-MDP);N-acetyl-nor-muramyl-L-alanyl-D-isoglutamine (CGP 11637, referred to asnor-MDP);N-acetylmuramyl-L-alanyl-D-isoglutaminyl-L-alanine-2-(1′-2′-dipalmitoyl-sn-glycero-3-hydroxyphos-phoryloxy)-ethylamine(CGP 19835A, referred to a MTP-PE); RIBI, which contains threecomponents from bacteria; monophosphoryl lipid A; trehalose dimycoloate;cell wall skeleton (MPL+TDM+CWS) in a 2% squalene/Tween 80 emulsion; andcholera toxin. Others which may be used are non-toxic derivatives ofcholera toxin, including its B subunit, and/or conjugates or geneticallyengineered fusions of the S. pneumoniae polypeptide with cholera toxinor its B subunit, procholeragenoid, fungal polysaccharides, includingschizophyllan, muramyl dipeptide, muramyl dipeptide derivatives, phorbolesters, labile toxin of E. coli, non-S. pneumoniae bacterial lysates,block polymers or saponins.

Other suitable delivery methods include biodegradable microcapsules orimmuno-stimulating complexes (ISCOMs), cochleates, or liposomes,genetically engineered attenuated live vectors such as viruses orbacteria, and recombinant (chimeric) virus-like particles, e.g.,bluetongue. The amount of adjuvant employed will depend on the type ofadjuvant used. For example, when the mucosal adjuvant is cholera toxin,it is suitably used in an amount of 5 mg to 50 mg, for example 10 mg to35 mg. When used in the form of microcapsules, the amount used willdepend on the amount employed in the matrix of the microcapsule toachieve the desired dosage. The determination of this amount is withinthe skill of a person of ordinary skill in the art.

Carrier systems in humans may include enteric release capsulesprotecting the antigen from the acidic environment of the stomach, andincluding S. pneumoniae polypeptide in an insoluble form as fusionproteins. Suitable carriers for the vaccines of the invention areenteric coated capsules and polylactide-glycolide microspheres. Suitablediluents are 0.2 N NaHCO3 and/or saline.

Vaccines of the invention can be administered as a primary prophylacticagent in adults or in children, as a secondary prevention, aftersuccessful eradication of S. pneumoniae in an infected host, or as atherapeutic agent in the aim to induce an immune response in asusceptible host to prevent infection by S. pneumoniae. The vaccines ofthe invention are administered in amounts readily determined by personsof ordinary skill in the art. Thus, for adults a suitable dosage will bein the range of 10 mg to 10 g, preferably 10 mg to 100 mg. A suitabledosage for adults will also be in the range of 5 mg to 500 mg. Similardosage ranges will be applicable for children. Those skilled in the artwill recognize that the optimal dose may be more or less depending uponthe patient's body weight, disease, the route of administration, andother factors. Those skilled in the art will also recognize thatappropriate dosage levels can be obtained based on results with knownoral vaccines such as, for example, a vaccine based on an E. coli lysate(6 mg dose daily up to total of 540 mg) and with an enterotoxigenic E.coli purified antigen (4 doses of 1 mg) (Schulman et al., J. Urol.150:917-921 (1993); Boedecker et al., American GastroenterologicalAssoc. 999:A-222 (1993)). The number of doses will depend upon thedisease, the formulation, and efficacy data from clinical trials.Without intending any limitation as to the course of treatment, thetreatment can be administered over 3 to 8 doses for a primaryimmunization schedule over 1 month (Boedeker, AmericanGastroenterological Assoc. 888:A-222 (1993)).

In a preferred embodiment, a vaccine composition of the invention can bebased on a killed whole E. coli preparation with an immunogenic fragmentof an S. pneumoniae protein of the invention expressed on its surface orit can be based on an E. coli lysate, wherein the killed E. coli acts asa carrier or an adjuvant.

It will be apparent to those skilled in the art that some of the vaccinecompositions of the invention are useful only for preventing S.pneumoniae infection, some are useful only for treating S. pneumoniaeinfection, and some are useful for both preventing and treating S.pneumoniae infection. In a preferred embodiment, the vaccine compositionof the invention provides protection against S. pneumoniae infection bystimulating humoral and/or cell-mediated immunity against S. pneumoniae.It should be understood that amelioration of any of the symptoms of S.pneumoniae infection is a desirable clinical goal, including a lesseningof the dosage of medication used to treat S. pneumoniae-caused disease,or an increase in the production of antibodies in the serum or mucous ofpatients.

Antibodies Reactive with S. pneumoniae Polypeptides

The invention also includes antibodies specifically reactive with thesubject S. pneumoniae polypeptide. Anti-protein/anti-peptide antisera ormonoclonal antibodies can be made by standard protocols (See, forexample, Antibodies: A Laboratory Manual ed. by Harlow and Lane (ColdSpring Harbor Press: 1988)). A mammal such as a mouse, a hamster orrabbit can be immunized with an immunogenic form of the peptide.Techniques for conferring immunogenicity on a protein or peptide includeconjugation to carriers or other techniques well known in the art. Animmunogenic portion of the subject S. pneumoniae polypeptide can beadministered in the presence of adjuvant. The progress of immunizationcan be monitored by detection of antibody titers in plasma or serum.Standard ELISA or other immunoassays can be used with the immunogen asantigen to assess the levels of antibodies.

In a preferred embodiment, the subject antibodies are immunospecific forantigenic determinants of the S. pneumoniae polypeptides of theinvention, e.g. antigenic determinants of a polypeptide of the inventioncontained in the Sequence Listing, or a closely related human ornon-human mammalian homolog (e.g., 90% homologous, more preferably atleast 95% homologous). In yet a further preferred embodiment of theinvention, the anti-S. pneumoniae antibodies do not substantially crossreact (i.e., react specifically) with a protein which is for example,less than 80% percent homologous to a sequence of the inventioncontained in the Sequence Listing. By “not substantially cross react”,it is meant that the antibody has a binding affinity for anon-homologous protein which is less than 10 percent, more preferablyless than 5 percent, and even more preferably less than 1 percent, ofthe binding affinity for a protein of the invention contained in theSequence Listing. In a most preferred embodiment, there is nocross-reactivity between bacterial and mammalian antigens.

The term antibody as used herein is intended to include fragmentsthereof which are also specifically reactive with S. pneumoniaepolypeptides. Antibodies can be fragmented using conventional techniquesand the fragments screened for utility in the same manner as describedabove for whole antibodies. For example, F(ab′)₂ fragments can begenerated by treating antibody with pepsin. The resulting F(ab′)₂fragment can be treated to reduce disulfide bridges to produce Fab′fragments. The antibody of the invention is further intended to includebispecific and chimeric molecules having an anti-S. pneumoniae portion.

Both monoclonal and polyclonal antibodies (Ab) directed against S.pneumoniae polypeptides or S. pneumoniae polypeptide variants, andantibody fragments such as Fab′ and F(ab′)₂, can be used to block theaction of S. pneumoniae polypeptide and allow the study of the role of aparticular S. pneumoniae polypeptide of the invention in aberrant orunwanted intracellular signaling, as well as the normal cellularfunction of the S. pneumoniae and by microinjection of anti-S.pneumoniae polypeptide antibodies of the present invention.

Antibodies which specifically bind S. pneumoniae epitopes can also beused in immunohistochemical staining of tissue samples in order toevaluate the abundance and pattern of expression of S. pneumoniaeantigens. Anti S. pneumoniae polypeptide antibodies can be useddiagnostically in immuno-precipitation and immuno-blotting to detect andevaluate S. pneumoniae levels in tissue or bodily fluid as part of aclinical testing procedure. Likewise, the ability to monitor S.pneumoniae polypeptide levels in an individual can allow determinationof the efficacy of a given treatment regimen for an individual afflictedwith such a disorder. The level of an S. pneumoniae polypeptide can bemeasured in cells found in bodily fluid, such as in urine samples or canbe measured in tissue, such as produced by gastric biopsy. Diagnosticassays using anti-S. pneumoniae antibodies can include, for example,immunoassays designed to aid in early diagnosis of S. pneumoniaeinfections. The present invention can also be used as a method ofdetecting antibodies contained in samples from individuals infected bythis bacterium using specific S. pneumoniae antigens.

Another application of anti-S. pneumoniae polypeptide antibodies of theinvention is in the immunological screening of cDNA librariesconstructed in expression vectors such as 1gt11, 1gt18-23, 1ZAP, and1ORF8. Messenger libraries of this type, having coding sequencesinserted in the correct reading frame and orientation, can producefusion proteins. For instance, 1gt11 will produce fusion proteins whoseamino termini consist of β-galactosidase amino acid sequences and whosecarboxy termini consist of a foreign polypeptide. Antigenic epitopes ofa subject S. pneumoniae polypeptide can then be detected withantibodies, as, for example, reacting nitrocellulose filters lifted frominfected plates with anti-S. pneumoniae polypeptide antibodies. Phage,scored by this assay, can then be isolated from the infected plate.Thus, the presence of S. pneumoniae gene homologs can be detected andcloned from other species, and alternate isoforms (including splicingvariants) can be detected and cloned.

Kits Containing Nucleic Acids, Polypeptides or Antibodies of theInvention

The nucleic acid, polypeptides and antibodies of the invention can becombined with other reagents and articles to form kits. Kits fordiagnostic purposes typically comprise the nucleic acid, polypeptides orantibodies in vials or other suitable vessels. Kits typically compriseother reagents for performing hybridization reactions, polymerase chainreactions (PCR), or for reconstitution of lyophilized components, suchas aqueous media, salts, buffers, and the like. Kits may also comprisereagents for sample processing such as detergents, chaotropic salts andthe like. Kits may also comprise immobilization means such as particles,supports, wells, dipsticks and the like. Kits may also comprise labelingmeans such as dyes, developing reagents, radioisotopes, fluorescentagents, luminescent or chemiluminescent agents, enzymes, intercalatingagents and the like. With the nucleic acid and amino acid sequenceinformation provided herein, individuals skilled in art can readilyassemble kits to serve their particular purpose. Kits further caninclude instructions for use.

Bio Chips and Microarrays

The nucleic acid sequence of the present invention may be used to detectS. pneumoniae or other species of Streptococcus acid sequence using biochip technology. Bio chips containing arrays of nucleic acid sequencecan also be used to measure expression of genes of S. pneumoniae orother species of Streptococcus. For example, to diagnose a patient witha S. pneumoniae or other Streptococcus infection, a sample from a humanor animal can be used as a probe on a bio chip containing an array ofnucleic acid sequence from the present invention. In addition, a samplefrom a disease state can be compared to a sample from a non-diseasestate which would help identify a gene that is up-regulated or expressedin the disease state. This would provide valuable insight as to themechanism by which the disease manifests. Changes in gene expression canalso be used to identify critical pathways involved in drug transport ormetabolism, and may enable the identification of novel targets involvedin virulence or host cell interactions involved in maintenance of aninfection. Procedures using such techniques have been described by Brownet al., 1995, Science 270: 467-470.

Bio chips can also be used to monitor the genetic changes of potentialtherapeutic compounds including, deletions, insertions or mismatches.Once the therapeutic is added to the patient, changes to the geneticsequence can be evaluated for its efficacy. In addition, the nucleicacid sequence of the present invention can be used to determineessential genes in cell cycling. As described in Iyer et al., 1999(Science, 283:83-87) genes essential in the cell cycle can be identifiedusing bio chips. Furthermore, the present invention provides nucleicacid sequence which can be used with bio chip technology to understandregulatory networks in bacteria, measure the response to environmentalsignals or drugs as in drug screening, and study virulence induction.(Mons et al., 1998, Nature Biotechnology, 16: 45-48. Patents teachingthis technology include U.S. Pat. Nos. 5,445,934, 5,744,305, and5,800,992.

Drug Screening Assays Using S. pneumoniae Polypeptides

By making available purified and recombinant S. pneumoniae polypeptides,the present invention provides assays which can be used to screen fordrugs which are either agonists or antagonists of the normal cellularfunction, in this case, of the subject S. pneumoniae polypeptides, or oftheir role in intracellular signaling. Such inhibitors or potentiatorsmay be useful as new therapeutic agents to combat S. pneumoniaeinfections in humans. A variety of assay formats will suffice and, inlight of the present inventions, will be comprehended by the skilledartisan.

In many drug screening programs which test libraries of compounds andnatural extracts, high throughput assays are desirable in order tomaximize the number of compounds surveyed in a given period of time.Assays which are performed in cell-free systems, such as may be derivedwith purified or semi-purified proteins, are often preferred as“primary” screens in that they can be generated to permit rapiddevelopment and relatively easy detection of an alteration in amolecular target which is mediated by a test compound. Moreover, theeffects of cellular toxicity and/or bioavailability of the test compoundcan be generally ignored in the in vitro system, the assay instead beingfocused primarily on the effect of the drug on the molecular target asmay be manifest in an alteration of binding affinity with other proteinsor change in enzymatic properties of the molecular target. Accordingly,in an exemplary screening assay of the present invention, the compoundof interest is contacted with an isolated and purified S. pneumoniaepolypeptide.

Screening assays can be constructed in vitro with a purified S.pneumoniae polypeptide or fragment thereof, such as an S. pneumoniaepolypeptide having enzymatic activity, such that the activity of thepolypeptide produces a detectable reaction product. The efficacy of thecompound can be assessed by generating dose response curves from dataobtained using various concentrations of the test compound. Moreover, acontrol assay can also be performed to provide a baseline forcomparison. Suitable products include those with distinctive absorption,fluorescence, or chemiluminescence properties, for example, becausedetection may be easily automated. A variety of synthetic or naturallyoccurring compounds can be tested in the assay to identify those whichinhibit or potentiate the activity of the S. pneumoniae polypeptide.Some of these active compounds may directly, or with chemicalalterations to promote membrane permeability or solubility, also inhibitor potentiate the same activity (e.g., enzymatic activity) in whole,live S. pneumoniae cells.

Overexpression Assays

Overexpression assays are based on the premise that overproduction of aprotein would lead to a higher level of resistance to compounds thatselectively interfere with the function of that protein. Overexpressionassays may be used to identify compounds that interfere with thefunction of virtually any type of protein, including without limitationenzymes, receptors, DNA- or RNA-binding proteins, or any proteins thatare directly or indirectly involved in regulating cell growth.

Typically, two bacterial strains are constructed. One contains a singlecopy of the gene of interest, and a second contains several copies ofthe same gene. Identification of useful inhibitory compounds of thistype of assay is based on a comparison of the activity of a testcompound in inhibiting growth and/or viability of the two strains. Themethod involves constructing a nucleic acid vector that directs highlevel expression of a particular target nucleic acid. The vectors arethen transformed into host cells in single or multiple copies to producestrains that express low to moderate and high levels of protein encodingby the target sequence (strain A and B, respectively). Nucleic acidcomprising sequences encoding the target gene can, of course, bedirectly integrated into the host cell.

Large numbers of compounds (or crude substances which may contain activecompounds) are screened for their effect on the growth of the twostrains. Agents which interfere with an unrelated target equally inhibitthe growth of both strains. Agents which interfere with the function ofthe target at high concentration should inhibit the growth of bothstrains. It should be possible, however, to titrate out the inhibitoryeffect of the compound in the overexpressing strain. That is, if thecompound is affecting the particular target that is being tested, itshould be possible to inhibit the growth of strain A at a concentrationof the compound that allows strain B to grow.

Alternatively, a bacterial strain is constructed that contains the geneof interest under the control of an inducible promoter. Identificationof useful inhibitory agents using this type of assay is based on acomparison of the activity of a test compound in inhibiting growthand/or viability of this strain under both inducing and non-inducingconditions. The method involves constructing a nucleic acid vector thatdirects high-level expression of a particular target nucleic acid. Thevector is then transformed into host cells that are grown under bothnon-inducing and inducing conditions (conditions A and B, respectively).

Large numbers of compounds (or crude substances which may contain activecompounds) are screened for their effect on growth under these twoconditions. Agents that interfere with the function of the target shouldinhibit growth under both conditions. It should be possible, however, totitrate out the inhibitory effect of the compound in the overexpressingstrain. That is, if the compound is affecting the particular target thatis being tested, it should be possible to inhibit growth under conditionA at a concentration that allows the strain to grow under condition B.

Ligand-binding Assays

Many of the targets according to the invention have functions that havenot yet been identified. Ligand-binding assays are useful to identifyinhibitor compounds that interfere with the function of a particulartarget, even when that function is unknown. These assays are designed todetect binding of test compounds to particular targets. The detectionmay involve direct measurement of binding. Alternatively, indirectindications of binding may involve stabilization of protein structure ordisruption of a biological function. Non-limiting examples of usefulligand-binding assays are detailed below.

A useful method for the detection and isolation of binding proteins isthe Biomolecular Interaction Assay (BIAcore) system developed byPharmacia Biosensor and described in the manufacturer's protocol (LKBPharmacia, Sweden). The BIAcore system uses an affinity purifiedanti-GST antibody to immobilize GST-fusion proteins onto a sensor chip.The sensor utilizes surface plasmon resonance which is an opticalphenomenon that detects changes in refractive indices. In accordancewith the practice of the invention, a protein of interest is coated ontoa chip and test compounds are passed over the chip. Binding is detectedby a change in the refractive index (surface plasmon resonance).

A different type of ligand-binding assay involves scintillationproximity assays (SPA, described in U.S. Pat. No. 4,568,649).

Another type of ligand binding assay, also undergoing development, isbased on the fact that proteins containing mitochondrial targetingsignals are imported into isolated mitochondria in vitro (Hurt et al.,1985, Embo J. 4:2061-2068; Eilers and Schatz, Nature, 1986,322:228-231). In a mitochondrial import assay, expression vectors areconstructed in which nucleic acids encoding particular target proteinsare inserted downstream of sequences encoding mitochondrial importsignals. The chimeric proteins are synthesized and tested for theirability to be imported into isolated mitochondria in the absence andpresence of test compounds. A test compound that binds to the targetprotein should inhibit its uptake into isolated mitochondria in vitro.

Another ligand-binding assay is the yeast two-hybrid system (Fields andSong, 1989, Nature 340:245-246). The yeast two-hybrid system takesadvantage of the properties of the GAL4 protein of the yeastSaccharomyces cerevisiae. The GAL4 protein is a transcriptionalactivator required for the expression of genes encoding enzymes ofgalactose utilization. This protein consists of two separable andfunctionally essential domains: an N-terminal domain which binds tospecific DNA sequences (UAS_(G)); and a C-terminal domain containingacidic regions, which is necessary to activate transcription. The nativeGAL4 protein, containing both domains, is a potent activator oftranscription when yeast are grown on galactose media. The N-terminaldomain binds to DNA in a sequence-specific manner but is unable toactivate transcription. The C-terminal domain contains the activatingregions but cannot activate transcription because it fails to belocalized to UAS_(G). In the two-hybrid system, a system of two hybridproteins containing parts of GAL4: (1) a GAL4 DNA-binding domain fusedto a protein ‘X’ and (2) a GAL4 activation region fused to a protein‘Y’. If X and Y can form a protein-protein complex and reconstituteproximity of the GAL4 domains, transcription of a gene regulated byUAS_(G) occurs. Creation of two hybrid proteins, each containing one ofthe interacting proteins X and Y, allows the activation region ofUAS_(G) to be brought to its normal site of action.

The binding assay described in Fodor et al., 1991, Science 251:767-773,which involves testing the binding affinity of test compounds for aplurality of defined polymers synthesized on a solid substrate, may alsobe useful.

Compounds which bind to the polypeptides of the invention arepotentially useful as antibacterial agents for use in therapeuticcompositions.

Pharmaceutical formulations suitable for antibacterial therapy comprisethe antibacterial agent in conjunction with one or more biologicallyacceptable carriers. Suitable biologically acceptable carriers include,but are not limited to, phosphate-buffered saline, saline, deionizedwater, or the like. Preferred biologically acceptable carriers arephysiologically or pharmaceutically acceptable carriers.

The antibacterial compositions include an antibacterial effective amountof active agent. Antibacterial effective amounts are those quantities ofthe antibacterial agents of the present invention that affordprophylactic protection against bacterial infections or which result inamelioration or cure of an existing bacterial infection. Thisantibacterial effective amount will depend upon the agent, the locationand nature of the infection, and the particular host. The amount can bedetermined by experimentation known in the art, such as by establishinga matrix of dosages and frequencies and comparing a group ofexperimental units or subjects to each point in the matrix.

The antibacterial active agents or compositions can be formed intodosage unit forms, such as for example, creams, ointments, lotions,powders, liquids, tablets, capsules, suppositories, sprays, aerosols orthe like. If the antibacterial composition is formulated into a dosageunit form, the dosage unit form may contain an antibacterial effectiveamount of active agent. Alternatively, the dosage unit form may includeless than such an amount if multiple dosage unit forms or multipledosages are to be used to administer a total dosage of the active agent.Dosage unit forms can include, in addition, one or more excipient(s),diluent(s), disintegrant(s), lubricant(s), plasticizer(s), colorant(s),dosage vehicle(s), absorption enhancer(s), stabilizer(s),bactericide(s), or the like.

For general information concerning formulations, see, e.g., Gilman etal. (eds.), 1990, Goodman and Gilman's: The Pharmacological Basis ofTherapeutics, 8th ed., Pergamon Press; and Remington's PharmaceuticalSciences, 17th ed., 1990, Mack Publishing Co., Easton, Pa.; Avis et al.(eds.), 1993, Pharmaceutical Dosage Forms: Parenteral Medications,Dekker, New York; Lieberman et al (eds.), 1990, Pharmaceutical DosageForms: Disperse Systems, Dekker, New York.

The antibacterial agents and compositions of the present invention areuseful for preventing or treating S. pneumoniae infections. Infectionprevention methods incorporate a prophylactically effective amount of anantibacterial agent or composition. A prophylactically effective amountis an amount effective to prevent S. pneumoniae infection and willdepend upon the specific bacterial strain, the agent, and the host.These amounts can be determined experimentally by methods known in theart and as described above.

S. pneumoniae infection treatment methods incorporate a therapeuticallyeffective amount of an antibacterial agent or composition. Atherapeutically effective amount is an amount sufficient to ameliorateor eliminate the infection. The prophylactically and/or therapeuticallyeffective amounts can be administered in one administration or overrepeated administrations. Therapeutic administration can be followed byprophylactic administration, once the initial bacterial infection hasbeen resolved.

The antibacterial agents and compositions can be administered topicallyor systemically. Topical application is typically achieved byadministration of creams, ointments, lotions, or sprays as describedabove. Systemic administration includes both oral and parental routes.Parental routes include, without limitation, subcutaneous,intramuscular, intraperitoneal, intravenous, transdermal, inhalation andintranasal administration.

EXEMPLIFICATION

I. Cloning and Sequencing of S. pneumoniae DNA

S. pneumoniae chromosomal DNA was isolated according to a basic DNAprotocol outlined in Schleif R. F. and Wensink P. C., Practical Methodsin Molecular Biology, p. 98, Springer-Verlag, N.Y., 1981, with minormodifications. Briefly, cells were pelleted, resuspended in TE (10 mMTris, 1 mM EDTA, pH 7.6) and GES lysis buffer (5.1 M guanidiumthiocyanate, 0.1 M EDTA, pH 8.0, 0.5% N-laurylsarcosine) was added.Suspension was chilled and ammonium acetate (NH4Ac) was added to finalconcentration of 2.0 M. DNA was extracted, first with chloroform, thenwith phenol-chloroform, and reextracted with chloroform. DNA wasprecipitated with isopropanol, washed twice with 70% EtOH, dried andresuspended in TE.

Following isolation whole genomic S. pneumoniae DNA was nebulized(Bodenteich et al., Automated DNA Sequencing and Analysis (J. C. Venter,ed.), Academic Press, 1994) to a median size of 2000 bp. Afternebulization, the DNA was concentrated and separated on a standard 1%agarose gel. Several fractions, corresponding to approximate sizes1000-1500 bp, 1500-2000 bp, 2000-2500 bp, 2500-3000 bp, were excisedfrom the gel and purified by the GeneClean procedure (Bio101, Inc.).

The purified DNA fragments were then blunt-ended using T4 DNApolymerase. The healed DNA was then ligated to unique BstXI-linkeradapters (5′ GTCTTCACCACGGGG (SEQ ID NO: 5323) and 5′ GTGGTGAAGAC (SEQID NO: 5324) in 100-1000 fold molar excess). These linkers arecomplimentary to the BstXI-cut pMPX vectors, while the overhang is notself-complimentary. Therefore, the linkers will not concatemerize norwill the cut-vector religate itself easily. The linker-adopted insertswere separated from the unincorporated linkers on a 1% agarose gel andpurified using GeneClean. The linker-adopted inserts were then ligatedto each of 20 pMPX vectors to construct a series of “shotgun” subclonelibraries. Blunt ended vector was used for cloning into the PUC19vector. The vectors contain an out-of-frame lacZ gene at the cloningsite which becomes in-frame in the event that an adapter-dimer iscloned, allowing these to be avoided by their blue-color.

All subsequent steps were based either on the multiplex DNA sequencingprotocols outlined in Church G. M. and Kieffer-Higgins S., Science240:185-188, 1988 or by ABI377 automated DNA sequencing methods. Onlymajor modifications to the protocols are highlighted. Briefly, each ofthe 20 vectors was then transformed into DH5a competent cells(Gibco/BRL, DH5a transformation protocol). The libraries were assessedby plating onto antibiotic plates containing ampicillin, methicillin andIPTG/Xgal. The plates were incubated overnight at 37° C. Successfultransformants were then used for plating of clones and pooling into themultiplex pools. The clones were picked and pooled into 40 ml growthmedium cultures. The cultures were grown overnight at 37° C. DNA waspurified using the Qiagen Midi-prep kits and Tip-100 columns (Qiagen,Inc.). In this manner, 100 mg of DNA was obtained per pool.

These purified DNA samples were then sequenced either using themultiplex DNA sequencing based on chemical degradation methods (ChurchG. M. and Kieffer-Higgins S., Science 240:185-188, 1988) or bySequithrem (Epicenter Technologies) dideoxy sequencing protocols or byABI dye-terminator chemistry. For the multiplex portion the sequencingreactions were electrophoresed and transferred onto nylon membranes bydirect transfer electrophoresis from 40 cm gels (Richterich P. andChurch G. M., Methods in Enzymology 218:187-222, 1993). The DNA wascovalently bound to the membranes by exposure to ultraviolet light, andhybridized with labeled oligonucleotides complimentary to tag sequenceson the vectors (Church, supra). The membranes were washed to rinse offnon-specifically bound probe, and exposed to X-ray film to visualizeindividual sequence ladders. After autoradiography, the hybridized probewas removed by incubation at 65° C., and the hybridization cyclerepeated with another tag sequence until the membrane had been probed 41times. Thus, each gel produced a large number of films, each containingnew sequencing information. Whenever a new blot was processed, it wasinitially probed for an internal standard sequence added to each of thepools. Digital images of the films were generated using a laser-scanningdensitometer (Molecular Dynamics, Sunnyvale, Calif.). The digitizedimages were processed on computer workstations (VaxStation 4000's) usingthe program REPLICA™ (Church et al., Automated DNA Sequencing andAnalysis (J. C. Venter, ed.), Academic Press, 1994). Image processingincluded lane straightening, contrast adjustment to smooth out intensitydifferences, and resolution enhancement by iterative gaussiandeconvolution. The sequences were then converted to an SCF format sothat processing and assembly could proceed on UNIX machines. The ABI dyeterminator sequence reads were run on ABI377 machines and the data wasdirectly transferred to UNIX machines following lane tracking of thegels. All multiplex and ABI reads were assembled using PHRAP (P. Green,Abstracts of DOE Human Genome Program Contractor-Grantee Workshop V,January 1996, p. 157) with default parameters and not using qualityscores. The initial assembly was done at 7fold coverage and yielded 511contigs. Short read length fragments of 200 bp or less found on the endsof contigs facing in the appropriate direction were used to extend offthe end of the contigs. These reads were then resequenced with primersusing ABI technology to give sequences with a read length of 500 or morebases. This allowed end extensions to be performed without ordering newprimers. In addition, missing mates (sequences from clones that onlygave one strand reads) were identified and sequenced with ABI technologyto allow the identification of additional overlapping contigs.

End-sequencing of randomly picked genomic lambda was also performed.Sequencing on a both sides was done for all lambda sequences. The lambdalibrary backbone helped to verify the integrity of the assembly andallowed closure of some of the physical gaps.

To identify S. pneumoniae polypeptides the complete genomic sequence ofS. pneumoniae were analyzed essentially as follows: First, all possiblestop-to-stop open reading frames (ORFs) greater than 180 nucleotides inall six reading frames were translated into amino acid sequences.Second, the identified ORFs were analyzed for homology to known(archeabacter, prokaryotic and eukaryotic) protein sequences. Third, thepredicted coding regions of the sequences and start codons wereevaluated with the programs GENEMARK™ (Borodovsky and McIninch, 1993,Comp. Chem. 17:123) and Glimmer (Fraser et al, Nature, 1997).

Identification Cloning and Expression of S. pneumoniae Nucleic Acids

Expression and purification of the S. pneumoniae polypeptides of theinvention can be performed essentially as outlined below.

To facilitate the cloning, expression and purification of membrane andsecreted proteins from S. pneumoniae, a gene expression system, such asthe pET System (Novagen), for cloning and expression of recombinantproteins in E. coli, is selected. Also, a DNA sequence encoding apeptide tag, the His-Tag, is fused to the 3′ end of DNA sequences ofinterest in order to facilitate purification of the recombinant proteinproducts. The 3′ end is selected for fusion in order to avoid alterationof any 5′ terminal signal sequence.

PCR Amplification and Cloning of Nucleic Acids Containing ORF's EncodingEnzymes

Nucleic acids chosen (for example, from the nucleic acids set forth inSEQ ID NO: 1-SEQ ID NO: 2661) for cloning from the 14453 strain of S.pneumoniae are prepared for amplification cloning by polymerase chainreaction (PCR). Synthetic oligonucleotide primers specific for the 5′and 3′ ends of open reading frames (ORFs) are designed and purchasedfrom GibcoBRL Life Technologies (Gaithersburg, Md., USA). All forwardprimers (specific for the 5′ end of the sequence) are designed toinclude an NcoI cloning site at the extreme 5′ terminus. These primersare designed to permit initiation of protein translation at a methionineresidue followed by a valine residue and the coding sequence for theremainder of the native S. pneumoniae DNA sequence. All reverse primers(specific for the 3′ end of any S. pneumoniae ORF) include a EcoRI siteat the extreme 5′ terminus to permit cloning of each S. pneumoniaesequence into the reading frame of the pET-28b. The pET-28b vectorprovides sequence encoding an additional 20 carboxy-terminal amino acidsincluding six histidine residues (at the extreme C-terminus), whichcomprise the His-Tag.

Genomic DNA prepared from strain 14453 of S. pneumoniae is used as thesource of template DNA for PCR amplification reactions (CurrentProtocols in Molecular Biology, John Wiley and Sons, Inc., F. Ausubel etal., eds., 1994). To amplify a DNA sequence containing an S. pneumoniaeORF, genomic DNA (50 nanograms) is introduced into a reaction vialcontaining 2 mM MgCl₂, 1 micromolar synthetic oligonucleotide primers(forward and reverse primers) complementary to and flanking a defined S.pneumoniae ORF, 0.2 mM of each deoxynucleotide triphosphate; dATP, dGTP,dCTP, dTTP and 2.5 units of heat stable DNA polymerase (Amplitaq, RocheMolecular Systems, Inc., Branchburg, N.J., USA) in a final volume of 100microliters.

Upon completion of thermal cycling reactions, each sample of amplifiedDNA is washed and purified using the Qiaquick Spin PCR purification kit(Qiagen, Gaithersburg, Md., USA). All amplified DNA samples aresubjected to digestion with the restriction endonucleases, e.g., NcoIand EcoRI (New England BioLabs, Beverly, Mass., USA)(Current Protocolsin Molecular Biology, John Wiley and Sons, Inc., F. Ausubel et al.,eds., 1994). DNA samples are then subjected to electrophoresis on 1.0%NuSeive (FMC BioProducts, Rockland, Me. USA) agarose gels. DNA isvisualized by exposure to ethidium bromide and long wave uv irradiation.DNA contained in slices isolated from the agarose gel is purified usingthe Bio 101 GeneClean Kit protocol (Bio 101 Vista, Calif., USA).

Cloning of S. pneumoniae Nucleic Acids into an Expression Vector

The pET-28b vector is prepared for cloning by digestion withendonucleases, e.g., NcoI and EcoRI (Current Protocols in MolecularBiology, John Wiley and Sons, Inc., F. Ausubel et al., eds., 1994). ThepET-28a vector, which encodes a His-Tag that can be fused to the 5′ endof an inserted gene, is prepared by digestion with appropriaterestriction endonucleases.

Following digestion, DNA inserts are cloned (Current Protocols inMolecular Biology, John Wiley and Sons, Inc., F. Ausubel et al., eds.,1994) into the previously digested pET-28b expression vector. Productsof the ligation reaction are then used to transform the BL21 strain ofE. coli (Current Protocols in Molecular Biology, John Wiley and Sons,Inc., F. Ausubel et al., eds., 1994) as described below.

Transformation of Competent Bacteria with Recombinant Plasmids

Competent bacteria, E coli strain BL21 or E. coli strain BL21 (DE3), aretransformed with recombinant pET expression plasmids carrying the clonedS. pneumoniae sequences according to standard methods (Current Protocolsin Molecular, John Wiley and Sons, Inc., F. Ausubel et al., eds., 1994).Briefly, 1 microliter of ligation reaction is mixed with 50 microlitersof electrocompetent cells and subjected to a high voltage pulse, afterwhich, samples are incubated in 0.45 milliliters SOC medium (0.5% yeastextract, 2.0% tryptone, 10 mM NaCl, 2.5 mM KCl, 10 mM MgCl2, 10 mM MgSO4and 20, mM glucose) at 37° C. with shaking for 1 hour. Samples are thenspread on LB agar plates containing 25 microgram/ml kanamycin sulfatefor growth overnight. Transformed colonies of BL21 are then picked andanalyzed to evaluate cloned inserts as described below.

Identification of Recombinant Expression Vectors with S. pneumoniaeNucleic Acids

Individual BL21 clones transformed with recombinant pET-28b S.pneumoniae ORFs are analyzed by PCR amplification of the cloned insertsusing the same forward and reverse primers, specific for each S.pneumoniae sequence, that were used in the original PCR amplificationcloning reactions. Successful amplification verifies the integration ofthe S. pneumoniae sequences in the expression vector (Current Protocolsin Molecular Biology, John Wiley and Sons, Inc., F. Ausubel et al.,eds., 1994).

Isolation and Preparation of Nucleic Acids from Transformants

Individual clones of recombinant pET-28b vectors carrying properlycloned S. pneumoniae ORFs are picked and incubated in 5 mls of LB brothplus 25 microgram/ml kanamycin sulfate overnight. The following dayplasmid DNA is isolated and purified using the Qiagen plasmidpurification protocol (Qiagen Inc., Chatsworth, Calif., USA).

Expression of Recombinant S. pneumoniae Sequences in E. coli

The pET vector can be propagated in any E. coli K-12 strain e.g. HMS174,HB101, JM109, DH5, etc. for the purpose of cloning or plasmidpreparation. Hosts for expression include E. coli strains containing achromosomal copy of the gene for T7 RNA polymerase. These hosts arelysogens of bacteriophage DE3, a lambda derivative that carries the lacIgene, the lacUV5 promoter and the gene for T7 RNA polymerase. T7 RNApolymerase is induced by addition of isopropyl-B-D-thiogalactoside(IPTG), and the T7 RNA polymerase transcribes any target plasmid, suchas pET-28b, carrying its gene of interest. Strains used include:BL21(DE3) (Studier, F. W., Rosenberg, A. H., Dunn, J. J., andDubendorff, J. W. (1990) Meth. Enzymol. 185, 60-89).

To express recombinant S. pneumoniae sequences, 50 nanograms of plasmidDNA isolated as described above is used to transform competent BL21(DE3) bacteria as described above (provided by Novagen as part of thepET expression system kit). The lacZ gene (beta-galactosidase) isexpressed in the pET-System as described for the S. pneumoniaerecombinant constructions. Transformed cells are cultured in SOC mediumfor 1 hour, and the culture is then plated on LB plates containing 25micrograms/ml kanamycin sulfate. The following day, bacterial coloniesare pooled and grown in LB medium containing kanamycin sulfate (25micrograms/ml) to an optical density at 600 nM of 0.5 to 1.0 O.D. units,at which point, 1 millimolar IPTG was added to the culture for 3 hoursto induce gene expression of the S. pneumoniae recombinant DNAconstructions.

After induction of gene expression with IPTG, bacteria are pelleted bycentrifugation in a Sorvall RC-3B centrifuge at 3500×g for 15 minutes at4° C. Pellets are resuspended in 50 milliliters of cold 10 mM Tris-HCl,pH 8.0, 0.1 M NaCl and 0.1 mM EDTA (STE buffer). Cells are thencentrifuged at 2000×g for 20 min at 4° C. Wet pellets are weighed andfrozen at −80° C. until ready for protein purification.

A variety of methodologies known in the art can be utilized to purifythe isolated proteins. (Current Protocols in Protein Science, John Wileyand Sons, Inc., J. E. Coligan et al., eds., 1995). For example, thefrozen cells may be thawed, resupended in buffer and ruptured by severalpassages through a small volume microfluidizer (Model M-110S,Microfluidics International Corporation, Newton, Mass.). The resultanthomogenate may be centrifuged to yield a clear supernatant (crudeextract) and following filtration the crude extract may be fractionatedover columns. Fractions may be monitored by absorbance at OD₂₈₀ nm. andpeak fractions may analyzed by SDS-PAGE

The concentrations of purified protein preparations may be quantifiedspectrophotometrically using absorbance coefficients calculated fromamino acid content (Perkins, S. J. 1986 Eur. J. Biochem. 157, 169-180).Protein concentrations are also measured by the method of Bradford, M.M. (1976) Anal. Biochem. 72, 248-254, and Lowry, O. H., Rosebrough, N.,Farr, A. L. & Randall, R. J. (1951) J. Biol. Chem. 193, pages 265-275,using bovine serum albumin as a standard.

SDS-polyacrylamide gels of various concentrations may be purchased fromBioRad (Hercules, Calif., USA), and stained with Coomassie blue.Molecular weight markers may include rabbit skeletal muscle myosin (200kDa), E. coli (-galactosidase (116 kDa), rabbit muscle phosphorylase B(97.4 kDa), bovine serum albumin (66.2 kDa), ovalbumin (45 kDa), bovinecarbonic anhydrase (31 kDa), soybean trypsin inhibitor (21.5 kDa), eggwhite lysozyme (14.4 kDa) and bovine aprotinin (6.5 kDa).

EQUIVALENTS

While this invention has been particularly shown and described withreferences to preferred embodiments thereof, it will be understood bythose skilled in the art that various changes in form and details may bemade therein without departing from the scope of the inventionencompassed by the appended claims.

ORF NAME NT ID AA ID AA LN NT LN SCORE P-VALUE DESCRIPTION SPX0001 12662 111 333 552 2.20E-74 [GI:2804700] [LN:AF030361] [AC:AF030361][PN:transposase] [OR:Streptococcus pneumoniae] 87 SPX0002 2 2663 173 519885 3.60E-120 [GI:663278] [LN:STRCOMAA] [AC:M36180:L15190][PN:transposase] [OR:Streptococcus pneumoniae] [SR:Streptococcuspneumoniae (strain RX1) DNA] 138 SPX0003 3 2664 109 327 281 1.40E-34[GI:2804700] [LN:AF030361] [AC:AF030361] [PN:transposase][OR:Streptococcus pneumoniae] 87 SPX0004 4 2665 190 570 948 7.40E-131[GI:663279] [LN:STRCOMAA] [AC:M36180:L15190] [PN:transposase][OR:Streptococcus pneumoniae] [SR:Streptococcus pneumoniae (strain RX1)DNA] 138 SPX0005 5 2666 122 366 NO-HIT 6 SPX0006 6 2667 401 1203 8157.40E-125 [LN:RS1_LEULA] [AC:P50889:P71450] [GN:RPS1] [OR:Leuconostoclactis] [DE:40S RIBOSOMAL PROTEIN S1] [SP:P50889:P71450] 116 SPX0007 72668 79 237 89 2.90E-05 [LN:E64801] [AC:E64801] [PN:hypothetical proteinb0663] [OR:Escherichia coli] 77 SPX0008 8 2669 77 231 NO-HIT 6 SPX0009 92670 215 645 832 6.30E-114 [LN:PCP_STRPY] [AC:Q01328] [GN:PCP][OR:Streptococcus pyogenes] [EC:3.4.19.3] [DE:PEPTIDASE)(PYROGLUTAMYL-PEPTIDASE I) (PGP-I) (PYRASE)] [SP:Q01328] 149 SPX0010 102671 308 924 234 3.90E-61 [LN:A81402] [AC:A81402] [PN:probable integralmembrane protein Cj0553 [imported]] [GN:Cj0553] [OR:Campylobacterjejuni] 119 SPX0011 11 2672 237 711 208 1.30E-37 [GI:6002226] [LN:SC51A][AC:AL121596] [PN:possible integral membrane protein] [GN:SCF51A.18c][OR:Streptomyces coelicolor A3(2)] 128 SPX0012 12 2673 235 705 2131.30E-53 [GI:2804687] [LN:AF030359] [AC:AF030359] [PN:oligopeptidebinding protein] [GN:aliA] [OR:Streptococcus pneumoniae] 114 SPX0013 132674 341 1023 1359 9.60E-184 [GI:6979306] [LN:AF164204] [AC:AF164204][PN:branched-chain amino acid aminotransferase] [GN:bcaT] [FN:catalyzesthe first reaction in the catabolism] [OR:Lactococcus lactis subsp.cremoris] 190 SPX0014 14 2675 824 2472 4143 0 [GI:6851038][LN:SPPARCETP] [AC:Z67739] [PN:DNA topoisomerase IV] [GN:parC][OR:Streptococcus pneumoniae] 105 SPX0015 15 2676 648 1944 3318 0[GI:6851037] [LN:SPPARCETP] [AC:Z67739] [PN:DNA topoisomerase IV][GN:parE] [OR:Streptococcus pneumoniae] 105 SPX0016 16 2677 214 642 10732.50E-150 [LN:YPAE_STRPN] [AC:Q54916] [OR:Streptococcus pneumoniae][DE:HYPOTHETICAL 23.0 KD PROTEIN IN PARE 5′REGION (ORF2)] [SP:Q54916]127 SPX0017 17 2678 410 1230 1044 8.20E-270 [GI:2804700] [LN:AF030361][AC:AF030361] [PN:transposase] [OR:Streptococcus pneumoniae] 87 SPX001818 2679 278 834 591 9.50E-139 [LN:A33595] [AC:A33595:A30868][PN:probable transposase] [CL:transposase IS3] [OR:Streptococcusagalactiae] 107 SPX0019 19 2680 191 573 422 2.30E-53 [LN:B30868][AC:B30868] [PN:hypothetical protein 1] [OR:Streptococcus agalactiae] 81SPX0020 20 2681 34 102 124 5.30E-12 [LN:B30868] [AC:B30868][PN:hypothetical protein 1] [OR:Streptococcus agalactiae] 81 SPX0021 212682 319 957 1002 3.80E-138 [LN:F70009] [AC:F70009] [PN:conservedhypothetical protein yufQ] [GN:yufQ] [CL:probable ribose ABC transporterrbsC-2] [OR:Bacillus subtilis] 141 SPX0022 22 2683 362 1086 385 3.70E-85[LN:E70009] [AC:E70009] [PN:conserved hypothetical protein yufP][GN:yufP] [OR:Bacillus subtilis] 97 SPX0023 23 2684 512 1536 16232.30E-217 [LN:D70009] [AC:D70009] [PN:probable ABC transporter yufO][GN:yufO] [CL:Bacillus subtilis probable ABC transporteryufO:ATP-binding cassette homology] [OR:Bacillus subtilis] 174 SPX002424 2685 140 420 83 1.80E-06 [LN:G72493] [AC:G72493] [PN:hypotheticalprotein APE2590] [GN:APE2590] [OR:Aeropyrum pernix] 92 SPX0025 25 2686364 1092 354 8.80E-82 [LN:YUFN_BACSU] [AC:O05252] [GN:YUFN] [OR:Bacillussubtilis] [DE:HYPOTHETICAL LIPOPROTEIN YUFN PRECURSOR] [SP:O05252] 117SPX0026 26 2687 130 390 324 5.40E-40 [GI:6478520] [LN:AF187304][AC:AF187304] [PN:cytidine deaminase] [GN:cdd] [OR:Bacilluscaldolyticus] 100 SPX0027 27 2688 100 300 276 2.40E-33 [LN:D75424][AC:D75424] [PN:deoxyribose-phosphate aldolase] [GN:DR1205][CL:deoxyribose-phosphate aldolase] [OR:Deinococcus radiodurans] 136SPX0028 28 2689 61 183 NO-HIT 6 SPX0029 29 2690 119 357 344 3.30E-42[LN:DEOC_BACSU] [AC:P39121] [GN:DRA] [OR:Bacillus subtilis] [EC:4.1.2.4][DE:(DEOXYRIBOALDOLASE)] [SP:P39121] 109 SPX0030 30 2691 426 1278 9219.70E-147 [LN:PDP_BACST] [AC:P77836] [GN:PYN] [OR:Bacillusstearothermophilus] [EC:2.4.2.2] [DE:PYRIMIDINE-NUCLEOSIDEPHOSPHORYLASE, (PYNP)] [SP:P77836] 144 SPX0031 31 2692 197 591 2502.00E-56 [LN:S59955] [AC:S59955] [PN:hypothetical protein 202][CL:hypothetical protein MJ0882] [OR:Staphylococcus aureus] 113 SPX003232 2693 73 219 NO-HIT 6 SPX0033 33 2694 100 300 NO-HIT 6 SPX0034 34 2695317 951 345 3.80E-79 [GI:6960352] [LN:STYSTMF1] [AC:AF170176] [PN:96%identity over 316 amino acids with E. coli] [GN:coaA] [OR:Salmonellatyphimurium LT2] 134 SPX0035 35 2696 79 237 98 8.40E-17 [LN:R3EC20][AC:A30425:A02748:S40547:G64722:S07374] [PN:ribosomal protein S20/L26[validated]:ribosomal protein L26:ribosomal protein S20] [GN:rpsT][CL:Escherichia coli ribosomal protein S20] [OR:Escherichia coli] 214SPX0036 36 2697 175 525 270 6.30E-50 [GI:6434823] [LN:SPU78969][AC:U78969] [PN:FlaR] [GN:flaR] [OR:Streptococcus pyogenes] 86 SPX003737 2698 237 711 1042 4.10E-140 [LN:DEOD_STRTR] [AC:Q56037] [GN:DEOD][OR:Streptococcus thermophilus] [EC:2.4.2.1] [DE:(PNP) (FRAGMENT)][SP:Q56037] 116 SPX0038 38 2699 171 513 271 1.10E-30 [GI:6729344][LN:AB029317] [AC:AB029317] [PN:intermedilysin] [GN:ily][OR:Streptococcus intermedius] [SR:Streptococcus intermedius(strain:UNS46) DNA] 150 SPX0039 39 2700 192 576 117 2.80E-07[LN:PXN1_XENLA] [AC:P49263] [GN:PXN1] [OR:Xenopus laevis] [SR:,Africanclawed frog] [DE:PENTRAXIN FUSION PROTEIN PRECURSOR] [SP:P49263] 137SPX0040 40 2701 136 408 92 0.00026 [LN:CP23_CHICK] [AC:P23614][OR:Gallus gallus] [SR:,Chicken] [DE:23 KD CORTICALCYTOSKELETON-ASSOCIATED PROTEIN (CAP-23)] [SP:P23614] 135 SPX0041 412702 270 810 395 1.40E-105 [LN:DEOD_BACSU] [AC:P46354] [GN:DEOD:PNP][OR:Bacillus subtilis] [EC:2.4.2.1] [DE:(PNP)] [SP:P46354] 100 SPX004242 2703 181 543 NO-HIT 6 SPX0043 43 2704 404 1212 736 2.30E-199[LN:DEOB_LACLC] [AC:O32808] [GN:DEOB] [OR:Lactococcus lactis][SR:,subspcremoris:Streptococcus cremoris] [EC:5.4.2.7][DE:PHOSPHOPENTOMUTASE, (PHOSPHODEOXYRIBOMUTASE)] [SP:O32808] 181SPX0044 44 2705 247 741 206 1.40E-52 [LN:G69180] [AC:G69180] [PN:ribose5-phosphate isomerase] [GN:MTH608] [CL:Haemophilus influenzaeribose-5-phosphate isomerase] [OR:Methanobacterium thermoautotrophicum]168 SPX0045 45 2706 62 186 NO-HIT 6 SPX0046 46 2707 291 873 386 5.80E-99[LN:YFOL_STRTR] [AC:P96051] [OR:Streptococcus thermophilus][DE:(ORF1091)] [SP:P96051] 86 SPX0047 47 2708 307 921 1049 3.00E-140[LN:FOLD_STRTR] [AC:P96050] [GN:FOLD] [OR:Streptococcus thermophilus][EC:1.5.1.5:3.5.4.9] [DE:(EC 3.5.4.9)]] [SP:P96050] 121 SPX0048 48 270972 216 99 5.40E-08 [LN:G72510] [AC:G72510] [PN:hypothetical proteinAPE2061] [GN:APE2061] [OR:Aeropyrum pernix] 92 SPX0049 49 2710 245 735796 7.00E-105 [LN:H69334] [AC:H69334] [PN:glutamine transport proteinglnQ] [GN:glnQ] [CL:inner membrane protein malK:ATP-binding cassettehomology] [OR:Archaeoglobus fulgidus] 162 SPX0050 50 2711 128 384 885.60E-05 [LN:D72757] [AC:D72757] [PN:hypothetical protein APE0049][GN:APE0049] [OR:Aeropyrum pernix] 92 SPX0051 51 2712 228 684 3141.10E-52 [LN:H69278] [AC:H69278] [PN:glutamine ABC transporter, permeaseprotein (glnP) homolog] [CL:histidine permease protein M][OR:Archaeoglobus fulgidus] 151 SPX0052 52 2713 77 231 89 8.60E-09[LN:G69865] [AC:G69865] [PN:hypothetical protein ykuJ] [GN:ykuJ][OR:Bacillus subtilis] 87 SPX0053 53 2714 753 2259 2641 0 [GI:4103470][LN:AF023421] [AC:AF023421] [PN:ClpE] [GN:clpE] [OR:Lactococcus lactis]84 SPX0054 54 2715 83 249 116 9.50E-10 [GI:4098132] [LN:MBU73653][AC:U73653] [PN:63 kDa protein] [OR:Mycobacterium bovis] 83 SPX0055 552716 61 183 NO-HIT 6 SPX0056 56 2717 70 210 NO-HIT 6 SPX0057 57 2718 114342 477 2.00E-73 [GI:5019553] [LN:SPN239004] [AC:AJ239004] [PN:putativetransposase] [OR:Streptococcus pneumoniae] 97 SPX0058 58 2719 116 348569 6.90E-75 [GI:4200438] [LN:AF026471] [AC:AF026471] [PN:putativetransposase] [OR:Streptococcus pneumoniae] 96 SPX0059 59 2720 141 423101 5.60E-07 [LN:A70315] [AC:A70315] [PN:AP4A hydrolase] [GN:apfA][CL:Methanococcus jannaschii mutator protein mutT:mutT domain homology][OR:Aquifex aeolicus] 147 SPX0060 60 2721 100 300 NO-HIT 6 SPX0061 612722 198 594 597 3.80E-95 [LN:A33595] [AC:A33595:A30868] [PN:probabletransposase] [CL:transposase IS3] [OR:Streptococcus agalactiae] 107SPX0062 62 2723 88 264 308 1.70E-38 [LN:A33595] [AC:A33595:A30868][PN:probable transposase] [CL:transposase IS3] [OR:Streptococcusagalactiae] 107 SPX0063 63 2724 34 102 126 2.60E-12 [LN:B30868][AC:B30868] [PN:hypothetical protein 1] [OR:Streptococcus agalactiae] 81SPX0064 64 2725 117 351 210 5.10E-24 [LN:JC1151] [AC:JC1151][PN:hypothetical protein, 20.3K] [OR:Agrobacterium tumefaciens] 89SPX0065 65 2726 102 306 154 5.60E-19 [GI:722339] [LN:AXU22323][AC:U22323] [PN:unknown] [OR:Acetobacter xylinus] [SR:Acetobacterxylinum] 100 SPX0066 66 2727 89 267 NO-HIT 6 SPX0067 67 2728 576 1728285 5.20E-53 [LN:G70002] [AC:G70002] [PN:hypothetical protein ytwP][GN:ytwP] [OR:Bacillus subtilis] 87 SPX0068 68 2729 649 1947 3322 0[GI:1490397] [LN:SPGYRBORF] [AC:Z67740] [PN:DNA gyrase] [GN:gyrB][OR:Streptococcus pneumoniae] 95 SPX0069 69 2730 191 573 709 2.40E-93[GI:1052803] [LN:SPGYRBG] [AC:X83917] [GN:orflgyrb] [OR:Streptococcuspneumoniae] 81 SPX0070 70 2731 185 555 118 9.00E-28 [LN:D70177][AC:D70177] [PN:4-methyl-5(b-hydroxyethyl)-thiazole monophosphatebiosynthesis protein (thiJ) homolog] [CL:signal transduction proteinDJ-1] [OR:Borrelia burgdorferi] [SR:, Lyme disease spirochete] 211SPX0071 71 2732 417 1251 398 1.00E-50 [LN:S22738] [AC:S22738:S22728][PN:hypothetical protein] [OR:Streptococcus salivarius] 86 SPX0072 722733 817 2451 203 3.80E-66 [LN:DING_BACSU] [AC:P54394] [GN:DING][OR:Bacillus subtilis] [DE:PROBABLE ATP-DEPENDENT HELICASE DING HOMOLOG][SP:P54394] 122 SPX0073 73 2734 310 930 189 6.20E-42 [LN:G69979][AC:G69979] [PN:proteinase homolog yrrN] [GN:yrrN] [OR:Bacillussubtilis] 85 SPX0074 74 2735 96 288 NO-HIT 6 SPX0075 75 2736 445 13352202 4.50E-301 [LN:CIAH_STRPN] [AC:Q54955] [GN:CIAH] [OR:Streptococcuspneumoniae] [EC:2.7.3.-] [DE:SENSOR PROTEIN CIAH,] [SP:Q54955] 120SPX0076 76 2737 225 675 1130 1.70E-152 [LN:CIAR_STRPN] [AC:Q54954][GN:CIAR] [OR:Streptococcus pneumoniae] [DE:TRANSCRIPTIONAL REGULATORYPROTEIN CIAR] [SP:Q54954] 124 SPX0077 77 2738 849 2547 1653 0[GI:5524752] [LN:STH007700] [AC:AJ007700] [PN:aminopeptidase N][GN:pepN] [OR:Streptococcus thermophilus] 105 SPX0078 78 2739 147 441176 1.80E-20 [LN:T35570] [AC:T35570] [PN:hypothetical protein SC6G4.19cSC6G4.19c] [GN:SC6G4.19c] [OR:Streptomyces coelicolor] 113 SPX0079 792740 292 876 80 8.00E-10 [LN:PPSA_PYRFU] [AC:P42850:Q59672] [GN:PPSA][OR:Pyrococcus furiosus] [EC:2.7.9.2] [DE:DIKINASE) (PEP SYNTHASE)][SP:P42850:Q59672] 131 SPX0080 80 2741 243 729 NO-HIT 6 SPX0081 81 2742160 480 113 1.60E-07 [LN:C72513] [AC:C72513] [PN:hypothetical proteinAPE2080] [GN:APE2080] [OR:Aeropyrum pernix] 92 SPX0082 82 2743 76 228NO-HIT 6 SPX0083 83 2744 233 699 231 3.20E-28 [LN:GNO_GLUOX] [AC:P50199][GN:GNO] [OR:Gluconobacter oxydans] [EC:1.1.1.69] [DE:REDUCTASE)][SP:P50199] 104 SPX0084 84 2745 89 267 NO-HIT 6 SPX0085 85 2746 309 927210 2.40E-41 [LN:YDHF_ECOLI] [AC:P76187] [GN:YDHF] [OR:Escherichia coli][DE:HYPOTHETICAL OXIDOREDUCTASE IN SODC-NEMA INTERGENIC REGION][SP:P76187] 135 SPX0086 86 2747 272 816 114 3.70E-09 [GI:3043880][LN:LLU95841] [AC:U95841] [PN:transmembrane protein Tmp6][OR:Lactococcus lactis] 94 SPX0087 87 2748 72 216 146 1.50E-15[GI:3582220] [LN:AE001272] [AC:AE001272] [PN:conserved hypotheticalprotein] [GN:ORF00047] [OR:Lactococcus lactis] 114 SPX0088 88 2749 79237 NO-HIT 6 SPX0089 89 2750 82 246 269 2.80E-32 [LN:T30285] [AC:T30285][PN:hypothetical protein] [OR:Streptococcus pneumoniae] 79 SPX0090 902751 680 2040 734 6.10E-239 [LN:SYM_BACST] [AC:P23920] [GN:METS][OR:Bacillus stearothermophilus] [EC:6.1.1.10] [DE:(METRS)] [SP:P23920]108 SPX0091 91 2752 420 1260 287 2.30E-62 [LN:E69858] [AC:E69858][PN:conserved hypothetical protein yknZ] [GN:yknZ] [OR:Bacillussubtilis] 97 SPX0092 92 2753 234 702 663 9.00E-86 [GI:2822199][LN:SCU96166] [AC:U96166:AF227987] [PN:ATP-binding cassette protein][GN:tptC] [OR:Streptococcus cristatus] 120 SPX0093 93 2754 400 1200 1445.60E-36 [LN:C69858] [AC:C69858] [PN:conserved hypothetical proteinyknX] [GN:yknX] [OR:Bacillus subtilis] 97 SPX0094 94 2755 449 1347 7301.70E-192 [LN:S41386] [AC:S41386] [PN:glutathione reductase (NADPH),][CL:dihydrolipoamide dehydrogenase:dihydrolipoamide dehydrogenasehomology] [OR:Streptococcus thermophilus] [EC:1.6.4.2] 182 SPX0095 952756 179 537 218 6.90E-30 [LN:H72334] [AC:H72334] [PN:bioY protein][GN:TM0799] [OR:Thermotoga maritima] 78 SPX0096 96 2757 112 336 NO-HIT 6SPX0097 97 2758 80 240 171 1.50E-18 [LN:Y352_TREPA] [AC:O83371][GN:TP0352] [OR:Treponema pallidum] [DE:HYPOTHETICAL PROTEIN TP0352][SP:O83371] 108 SPX0098 98 2759 107 321 NO-HIT 6 SPX0099 99 2760 113 339109 1.40E-12 [GI:4098081] [LN:LLU73336] [AC:U73336] [PN:anaerobicribonucleotide reductase] [GN:nrdD] [OR:Lactococcus lactis subsp.cremoris] 128 SPX0100 100 2761 240 720 372 1.30E-85 [LN:TRMD_BACSU][AC:O31741] [GN:TRMD] [OR:Bacillus subtilis] [EC:2.1.1.31][DE:METHYLTRANSFERASE) (TRNA [GM37]METHYLTRANSFERASE)] [SP:O31741] 142SPX0101 101 2762 173 519 292 5.20E-61 [LN:RIMM_BACSU] [AC:O31740][GN:RIMM] [OR:Bacillus subtilis] [DE:PROBABLE 16S RRNA PROCESSINGPROTEIN RIMM] [SP:O31740] 119 SPX0102 102 2763 267 801 NO-HIT 6 SPX0103103 2764 80 240 141 9.70E-15 [LN:C69880] [AC:C69880] [PN:conservedhypothetical protein ylqC] [GN:ylqC] [CL:Bacillus conserved hypotheticalprotein ylqC] [OR:Bacillus subtilis] 147 SPX0104 104 2765 91 273 3155.10E-39 [LN:C47154] [AC:C47154:S11366:G69700] [PN:ribosomal protein S16(BS17) rpsP:ribosomal protein BS17] [GN:rpsP] [CL:Escherichia coliribosomal protein S16] [OR:Bacillus subtilis] 176 SPX0105 105 2766 70210 NO-HIT 6 SPX0106 106 2767 135 405 NO-HIT 6 SPX0107 107 2768 71 213NO-HIT 6 SPX0108 108 2769 268 804 243 3.60E-38 [LN:T41399] [AC:T41399][PN:probable cyclophilin-related peptidyl prolyl cis-trans isomerase][GN:SPCC553.04] [OR:Schizosaccharomyces pombe] 140 SPX0109 109 2770 120360 83 5.110E-05 [GI:1773206] [LN:ECU82664] [AC:U82664] [OR:Escherichiacoli] 60 SPX0110 110 2771 514 1542 1502 3.70E-258 [LN:D69813][AC:D69813] [PN:ABC transporter (ATP-binding protein) homolog yfmM][GN:yfmM] [CL:unassigned ATP-binding cassette proteins:ATP-bindingcassette homology] [OR:Bacillus subtilis] 188 SPX0111 111 2772 161 48388 2.20E-11 [GI:7110140] [LN:AF155139] [AC:AF155139:AF019976] [PN:VanZF][GN:vanZF] [OR:Paenibacillus popilliae] 100 SPX0112 112 2773 362 1086452 1.30E-135 [LN:YLON_BACSU] [AC:O34617] [GN:YLON] [OR:Bacillussubtilis] [DE:HYPOTHETICAL 41.6 KD PROTEIN IN FMT-SPOVM INTERGENICREGION] [SP:O34617] 137 SPX0113 113 2774 177 531 152 3.20E-25[LN:F70023] [AC:F70023] [PN:hypothetical protein yutD] [GN:yutD][CL:Bacillus subtilis hypothetical protein yutD] [OR:Bacillus subtilis]136 SPX0114 114 2775 202 606 1034 4.90E-138 [GI:5758312] [LN:AF162664][AC:AF162664] [PN:manganese co-factored superoxide dismutase] [GN:sodA][FN:removes superoxide] [OR:Streptococcus pneumoniae] 152 SPX0115 1152776 346 1038 952 2.60E-127 [GI:2765186] [LN:SASODA] [AC:Y12224][PN:hypothetical protein] [OR:Streptococcus agalactiae] 92 SPX0116 1162777 312 936 1616 3.20E-220 [GI:5578893] [LN:SPN131985] [AC:AJ131985][PN:dihydroorotate dehydrogenase] [GN:pyrDA] [OR:Streptococcuspneumoniae] 116 SPX0117 117 2778 397 1191 1399 3.90E-187 [LN:METK_STAAU][AC:P50307] [GN:METK] [OR:Staphylococcus aureus] [EC:2.5.1.6][DE:ADENOSYLTRANSFERASE) (ADOMET SYNTHETASE)] [SP:P50307] 135 SPX0118118 2779 448 1344 972 1.00E-140 [LN:YQFR_BACSU] [AC:P54475] [GN:YQFR][OR:Bacillus subtilis] [DE:PROBABLE RNA HELICASE IN CCCA-SODA INTERGENICREGION] [SP:P54475] 130 SPX0119 119 2780 272 816 NO-HIT 6 SPX0120 1202781 88 264 NO-HIT 6 SPX0121 121 2782 727 2181 735 4.60E-182[GI:4098489] [LN:SMU78600] [AC:U78600] [PN:putative ptsG protein][OR:Streptococcus mutans] 91 SPX0122 122 2783 312 936 330 2.80E-63[LN:G69627] [AC:G69627] [PN:cell-division protein ftsX] [GN:ftsX][OR:Bacillus subtilis] 88 SPX0123 123 2784 69 207 NO-HIT 6 SPX0124 1242785 231 693 798 9.90E-106 [LN:D69627] [AC:D69627] [PN:cell-divisionATP-binding protein ftsE] [GN:ftsE] [CL:unassigned ATP-binding cassetteproteins:ATP-binding cassette homology] [OR:Bacillus subtilis] 176SPX0125 125 2786 75 225 94 1.10E-07 [LN:A71007] [AC:A71007][PN:hypothetical protein PH1351] [GN:PH1351] [OR:Pyrococcus horikoshii]95 SPX0126 126 2787 307 921 936 6.80E-124 [LN:RF2_BACSU][AC:P28367:O34444] [GN:PRFB] [OR:Bacillus subtilis] [DE:PEPTIDE CHAINRELEASE FACTOR 2 (RF-2)] [SP:P28367:O34444] 128 SPX0127 127 2788 219 657279 3.40E-41 [LN:H72290] [AC:H72290] [PN:conserved hypothetical protein][GN:TM1140] [OR:Thermotoga maritima] 96 SPX0128 128 2789 237 711 7117.60E-93 [LN:T35757] [AC:T35757] [PN:probable branched chain amino acidtransport ATP-binding protein] [GN:SC7H2.26] [CL:unassigned ATP-bindingcassette proteins:ATP-binding cassette homology] [OR:Streptomycescoelicolor] 212 SPX0129 129 2790 67 201 109 6.60E-10 [LN:G72485][AC:G72485] [PN:hypothetical protein APE2527] [GN:APE2527] [OR:Aeropyrumpernix] 92 SPX0130 130 2791 255 765 387 4.20E-90 [LN:F72290] [AC:F72290][PN:branched chain amino acid ABC transporter, ATP-binding protein][GN:TM1138] [CL:unassigned ATP-binding cassette proteins:ATP-bindingcassette homology] [OR:Thermotoga maritima] 206 SPX0131 131 2792 319 957334 1.10E-63 [LN:E81303] [AC:E81303] [PN:probable branched-chainamino-acid ABC transport system permease protein Cj1016c [imported]][GN:livM:Cj1016c] [OR:Campylobacter jejuni] 164 SPX0132 132 2793 293 879325 1.30E-90 [LN:D72290] [AC:D72290] [PN:branched chain amino acid ABCtransporter, permease protein] [GN:TM1136] [CL:leucine transport proteinlivH] [OR:Thermotoga maritima] 163 SPX0133 133 2794 387 1161 1935.70E-39 [LN:H81303] [AC:H81303] [PN:branched-chain amino-acid ABCtransport system periplasmic binding protein Cj1019c [imported]][GN:livJ:Cj1019c] [OR:Campylobacter jejuni] 166 SPX0134 134 2795 150 450NO-HIT 6 SPX0135 135 2796 83 249 116 2.40E-11 [LN:D69874] [AC:D69874][PN:conserved hypothetical protein ylbG] [GN:ylbG] [OR:Bacillussubtilis] 97 SPX0136 136 2797 197 591 933 8.10E-124 [LN:CLPP_STRSL][AC:P36398] [GN:CLPP] [OR:Streptococcus salivarius] [EC:3.4.21.92][DE:(ENDOPEPTIDASE CLP)] [SP:P36398] 119 SPX0137 137 2798 217 651 9615.20E-129 [LN:UPP_STRSL] [AC:P36399] [GN:UPP] [OR:Streptococcussalivarius] [EC:2.4.2.9] [DE:PYROPHOSPHORYLASE) (UPRTASE)] [SP:P36399]124 SPX0138 138 2799 54 162 NO-HIT 6 SPX0139 139 2800 156 468 2654.40E-49 [LN:CME2_BACSU] [AC:P32393] [GN:COMEB:COME2] [OR:Bacillussubtilis] [DE:COME OPERON PROTEIN 2] [SP:P32393] 106 SPX0140 140 2801186 558 114 1.10E-07 [LN:G70325] [AC:G70325] [PN:transcription regulatorTetR/AcrR family] [GN:acrR3] [OR:Aquifex aeolicus] 102 SPX0141 141 2802282 846 813 2.60E-107 [GI:4580621] [LN:AF118389] [AC:AF118389][PN:unknown] [OR:Streptococcus suis] 77 SPX0142 142 2803 392 1176 3301.60E-83 [GI:2293312] [LN:AF008220] [AC:AF008220] [PN:YtfP] [GN:ytfP][OR:Bacillus subtilis] 83 SPX0143 143 2804 152 456 106 6.50E-12[LN:G70031] [AC:G70031] [PN:mutator MutT protein homolog yvcI] [GN:yvcI][CL:mutT domain homology] [OR:Bacillus subtilis] 121 SPX0144 144 2805173 519 876 2.10E-115 [GI:6179679] [LN:SPN239034] [AC:AJ239034][PN:regulator of pmrA] [GN:mta] [FN:regulator of pmrA expression][OR:Streptococcus pneumoniae] 137 SPX0145 145 2806 490 1470 8055.40E-151 [LN:F69825] [AC:F69825] [PN:sodium-dependent transporterhomolog yhdH] [GN:yhdH] [CL:gamma-aminobutyric acid transporter][OR:Bacillus subtilis] 144 SPX0146 146 2807 315 945 1165 3.00E-155[LN:MANA_STRMU] [AC:Q59935] [GN:PMI] [OR:Streptococcus mutans][EC:5.3.1.8] [DE:(PMI) (PHOSPHOHEXOMUTASE)] [SP:Q59935] 118 SPX0147 1472808 134 402 NO-HIT 6 SPX0148 148 2809 110 330 270 1.80E-43 [LN:JE0396][AC:JE0396] [PN:phospho-beta-galactosidase II] [CL:Agrobacteriumbeta-glucosidase] [OR:Lactobacillus gasseri] 121 SPX0149 149 2810 89 267NO-HIT 6 SPX0150 150 2811 218 654 154 1.00E-20 [GI:722339] [LN:AXU22323][AC:U22323] [PN:unknown] [OR:Acetobacter xylinus] [SR:Acetobacterxylinum] 100 SPX0151 151 2812 116 348 NO-HIT 6 SPX0152 152 2813 592 17763033 0 [LN:POXB_STRPN] [AC:Q54970] [GN:SPXB] [OR:Streptococcuspneumoniae] [EC:1.2.3.3] [DE:PYRUVATE OXIDASE, (PYRUVIC OXIDASE) (POX)][SP:Q54970] 141 SPX0153 153 2814 67 201 149 2.30E-14 [GI:1513069][LN:LMU15554] [AC:U15554] [PN:P-type adenosine triphosphatase] [GN:ctpA][FN:involved in cation transport] [OR:Listeria monocytogenes] 147SPX0154 154 2815 733 2199 648 8.80E-202 [GI:1513069] [LN:LMU15554][AC:U15554] [PN:P-type adenosine triphosphatase] [GN:ctpA] [FN:involvedin cation transport] [OR:Listeria monocytogenes] 147 SPX0155 155 2816 85255 107 2.40E-09 [LN:H72624] [AC:H72624] [PN:hypothetical proteinAPE1456] [GN:APE1456] [OR:Aeropyrum pernix] 92 SPX0156 156 2817 61 183NO-HIT 6 SPX0157 157 2818 124 372 70 6.10E-06 [LN:H69267] [AC:H69267][PN:cytochrome-c oxidase, chain II AF0144] [CL:cytochrome-c oxidasechain II:cytochrome-c oxidase chain II homology] [OR:Archaeoglobusfulgidus] [EC:1.9.3.1] 183 SPX0158 158 2819 142 426 240 1.00E-28[LN:COPY_ENTHR] [AC:Q47839] [GN:COPY] [OR:Enterococcus hirae] [DE:COPABATPASES METAL-FIST TYPE REPRESSOR] [SP:Q47839] 118 SPX0159 159 2820 269807 308 4.00E-99 [GI:6707002] [LN:AF109218] [AC:AF109218:U96108][PN:ThiD] [GN:thiD] [OR:Staphylococcus carnosus] 96 SPX0160 160 2821 211633 245 8.10E-55 [LN:D75087] [AC:D75087] [PN:thiamin phosphatepyrophosphorylase (thie) PAB1645] [GN:PAB1645] [CL:probablethiamin-phosphate pyrophosphorylase:thiamin-phosphate pyrophosphorylasehomology] [OR:Pyrococcus abyssi] 210 SPX0161 161 2822 269 807 2282.70E-27 [LN:THIM_ECOLI] [AC:P76423] [GN:THIM] [OR:Escherichia coli][EC:2.7.1.50] [DE:HYDROXYETHYLTHIAZOLE KINASE) (THZ KINASE) (TH KINASE)][SP:P76423] 144 SPX0162 162 2823 175 525 NO-HIT 6 SPX0163 163 2824 231693 384 2.00E-48 [LN:TENA_BACSU] [AC:P25052] [GN:TENA] [OR:Bacillussubtilis] [DE:TRANSCRIPTIONAL ACTIVATOR TENA] [SP:P25052] 108 SPX0164164 2825 217 651 112 1.10E-13 [GI:1296823] [LN:LHPEPIGN] [AC:Z56283][GN:orf2] [OR:Lactobacillus helveticus] 78 SPX0165 165 2826 462 1386 2794.50E-59 [GI:1296822] [LN:LHPEPIGN] [AC:Z56283] [GN:orf1][OR:Lactobacillus helveticus] 78 SPX0166 166 2827 187 561 203 2.20E-27[LN:A69859] [AC:A69859] [PN:hypothetical protein ykoE] [GN:ykoE][OR:Bacillus subtilis] 87 SPX0167 167 2828 75 225 NO-HIT 6 SPX0168 1682829 69 207 NO-HIT 6 SPX0169 169 2830 210 630 520 4.10E-72 [GI:6707004][LN:AF109218] [AC:AF109218:U96108] [PN:ThiE] [GN:thiE][OR:Staphylococcus carnosus] 96 SPX0170 170 2831 268 804 523 4.60E-67[GI:6707003] [LN:AF109218] [AC:AF109218:U96108] [PN:ThiM] [GN:thiM][OR:Staphylococcus carnosus] 96 SPX0171 171 2832 137 411 114 2.00E-08[LN:H71057] [AC:H71057] [PN:hypothetical protein PH1158] [GN:PH1158][OR:Pyrococcus horikoshii] 95 SPX0172 172 2833 82 246 NO-HIT 6 SPX0173173 2834 75 225 203 1.90E-23 [LN:T30285] [AC:T30285] [PN:hypotheticalprotein] [OR:Streptococcus pneumoniae] 79 SPX0174 174 2835 223 669 1276.60E-15 [LN:PT18_YEAST] [AC:P25362] [GN:PET18:HIT2:YCR020C:YCR20C][OR:Saccharomyces cerevisiae] [SR:,Baker′s yeast] [DE:PET18 PROTEIN][SP:P25362] 141 SPX0175 175 2836 379 1137 1379 5.20E-216 [GI:2239174][LN:SILCT] [AC:Y07622] [PN:lactate oxidase] [GN:lctO] [FN:lactateutilisation] [OR:Streptococcus iniae] 116 SPX0176 176 2837 497 1491 11571.60E-228 [LN:SYK_BACSU] [AC:P37477] [GN:LYSS] [OR:Bacillus subtilis][EC:6.1.1.6] [DE:LYSYL-TRNA SYNTHETASE, (LYSINE--TRNA LIGASE) (LYSRS)][SP:P37477] 144 SPX0177 177 2838 227 681 351 2.10E-70 [LN:D71849][AC:D71849] [PN:amino acid ABC transporter, permease protein][GN:jhp1096] [CL:histidine permease protein M] [OR:Helicobacter pylori][SR:strain J99, , strain J99] [SR:strain J99, ] 195 SPX0178 178 2839 127381 279 2.10E-35 [LN:B64666] [AC:B64666] [PN:glutamine ABC transporter,permease protein] [CL:histidine permease protein M] [OR:Helicobacterpylori] 133 SPX0179 179 2840 96 288 249 4.10E-30 [LN:B64666] [AC:B64666][PN:glutamine ABC transporter, permease protein] [CL:histidine permeaseprotein M] [OR:Helicobacter pylori] 133 SPX0180 180 2841 71 213 925.90E-05 [GI:4163988] [LN:AF082511] [AC:AF082511] [PN:putativeATP-binding protein MglA] [GN:mglA] [OR:Treponema denticola] 114 SPX0181181 2842 169 507 531 5.00E-70 [LN:H81391] [AC:H81391] [PN:amino-acid ABCtransporter ATP-binding protein Cj0469 [imported]] [GN:Cj0469][OR:Campylobacter jejuni] 131 SPX0182 182 2843 67 201 72 3.30E-07[LN:G72510] [AC:G72510] [PN:hypothetical protein APE2061] [GN:APE2061][OR:Aeropyrum pernix] 92 SPX0183 183 2844 81 243 132 5.50E-12[GI:4204972] [LN:LLU60994] [AC:U60994] [FN:transport systems for basicamino acids and] [OR:Leuconostoc lactis] 111 SPX0184 184 2845 185 555531 1.40E-67 [LN:C81373] [AC:C81373] [PN:probable amino-acid transporterperiplasmic solute-binding protein Cj0982c [imported]] [GN:Cj0982c][OR:Campylobacter jejuni] 153 SPX0185 185 2846 216 648 353 6.60E-51[LN:YYBJ_BACSU] [AC:P37494] [GN:YYBJ] [OR:Bacillus subtilis][DE:INTERGENIC REGION] [SP:P37494] 95 SPX0186 186 2847 235 705 NO-HIT 6SPX0187 187 2848 68 204 NO-HIT 6 SPX0188 188 2849 269 807 NO-HIT 6SPX0189 189 2850 255 765 NO-HIT 6 SPX0190 190 2851 117 351 NO-HIT 6SPX0191 191 2852 211 633 1057 1.30E-140 [GI:4009484] [LN:AF068902][AC:AF068902] [PN:orotate phosphoribosyltransferase PyrE] [GN:pyrE][OR:Streptococcus pneumoniae] 124 SPX0192 192 2853 234 702 11731.80E-157 [GI:4009483] [LN:AF068902] [AC:AF068902][PN:orotidine-5′-decarboxylase PyrF] [GN:pyrF] [OR:Streptococcuspneumoniae] 117 SPX0193 193 2854 67 201 NO-HIT 6 SPX0194 194 2855 4001200 1946 3.00E-251 [GI:4009482] [LN:AF068902] [AC:AF068902] [PN:celldivision protein DivIB] [GN:divIB] [OR:Streptococcus pneumoniae] 114SPX0195 195 2856 148 444 110 2.20E-07 [GI:6473880] [LN:AB027890][AC:AB027890] [PN:Hypothetical protein] [GN:SPBC3D5.14C][OR:Schizosaccharomyces pombe] [SR:Schizosaccharomyces pombe (strain:968h90) DNA, clone:TA46] 180 SPX0196 196 2857 353 1059 1780 1.40E-242[GI:4009481] [LN:AF068902] [AC:AF068902][PN:undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc] [GN:murG][OR:Streptococcus pneumoniae] 131 SPX0197 197 2858 451 1353 22061.20E-297 [GI:4009480] [LN:AF068902] [AC:AF068902] [PN:D-glutamic acidadding enzyme MurD] [GN:murD] [OR:Streptococcus pneumoniae] 120 SPX0198198 2859 214 642 1062 1.20E-142 [GI:4009479] [LN:AF068902] [AC:AF068902][PN:unknown] [OR:Streptococcus pneumoniae] 83 SPX0199 199 2860 674 20222263 0 [GI:4009478] [LN:AF068902] [AC:AF068902] [PN:unknown][OR:Streptococcus pneumoniae] 83 SPX0200 200 2861 135 405 86 1.80E-05[GI:7576923] [LN:AF242367] [AC:AF242367] [PN:lactococcin 972] [GN:lclA][OR:Lactococcus lactis subsp. lactis] 109 SPX0201 201 2862 73 219 NO-HIT6 SPX0202 202 2863 85 255 89 2.50E-05 [LN:T20916] [AC:T20916][PN:hypothetical protein F14F8.3] [GN:F14F8.3] [OR:Caenorhabditiselegans] 98 SPX0203 203 2864 621 1863 1706 0 [LN:TYPA_BACSU] [AC:O07631][GN:TYPA] [OR:Bacillus subtilis] [DE:GTP-BINDING PROTEIN TYPA/BIPAHOMOLOG] [SP:O07631] 115 SPX0204 204 2865 242 726 154 3.00E-34[GI:7328274] [LN:SAY14816] [AC:Y14816] [PN:hypothetical protein][GN:ORF231] [OR:Staphylococcus aureus] 103 SPX0205 205 2866 66 198NO-HIT 6 SPX0206 206 2867 127 381 174 3.80E-28 [LN:YQHL_BACSU][AC:P54510] [GN:YQHL] [OR:Bacillus subtilis] [DE:HYPOTHETICAL 14.6 KDPROTEIN IN GCVT-SPOIIIAA INTERGENIC REGION] [SP:P54510] 141 SPX0207 2072868 74 222 158 1.80E-17 [LN:T44786] [AC:T44786] [PN:hypotheticalprotein 1 [imported]] [OR:Bacillus megaterium] 87 SPX0208 208 2869 303909 1241 5.30E-168 [LN:T44638] [AC:T44638] [PN:capsular polysaccharidebiosynthesis protein cpsY [imported]] [GN:cpsY] [CL:probabletranscription regulator lsyR] [OR:Streptococcus agalactiae] 172 SPX0209209 2870 252 756 476 5.30E-66 [LN:YQJQ_BACSU] [AC:P54554] [GN:YQJQ][OR:Bacillus subtilis] [EC:1.-.-.-] [DE:(EC 1.-.-.-)] [SP:P54554] 103SPX0210 210 2871 310 930 368 9.50E-98 [LN:YQJK_BACSU] [AC:P54548][GN:YQJK] [OR:Bacillus subtilis] [DE:HYPOTHETICAL 34.0 KD PROTEIN INGLNQ-ANSR INTERGENIC REGION] [SP:P54548] 137 SPX0211 211 2872 208 624NO-HIT 6 SPX0212 212 2873 413 1239 792 1.40E-103 [LN:B69888] [AC:B69888][PN:GTP-binding protein proteinase modulator homolog ynbA] [GN:ynbA][CL:GTP-binding protein hflX:translation elongation factor Tu homology][OR:Bacillus subtilis] 187 SPX0213 213 2874 312 936 317 7.10E-70[LN:G69657] [AC:G69657] [PN:tRNA isopentenylpyrophosphate transferasemiaA] [GN:miaA] [CL:delta(2)-isopentenylpyrophosphate transferase][OR:Bacillus subtilis] 159 SPX0214 214 2875 63 189 NO-HIT 6 SPX0215 2152876 66 198 129 6.10E-12 [LN:TYSY_LACLA] [AC:P19368] [GN:THYA][OR:Lactococcus lactis] [SR:,subsplactis:Streptococcus lactis][EC:2.1.1.45] [DE:THYMIDYLATE SYNTHASE, (TS)] [SP:P19368] 160 SPX0216216 2877 221 663 318 1.20E-39 [GI:7328278] [LN:SAY14816] [AC:Y14816][PN:hypothetical protein] [GN:ORF242] [OR:Staphylococcus aureus] 103SPX0217 217 2878 212 636 691 4.80E-91 [LN:B69997] [AC:B69997][PN:conserved hypothetical protein ytmQ] [GN:ytmQ] [CL:hypotheticalprotein HI0340] [OR:Bacillus subtilis] 130 SPX0218 218 2879 89 267NO-HIT 6 SPX0219 219 2880 103 309 215 6.90E-25 [LN:YLXS_BACSU][AC:P32726] [GN:YLXS] [OR:Bacillus subtilis] [DE:HYPOTHETICAL 17.6 KDPROTEIN IN NUSA 5′REGION (P15A) (ORF1)] [SP:P32726] 137 SPX0220 220 2881379 1137 715 6.00E-122 [GI:2634032] [LN:BSUB0009] [AC:Z99112:AL009126][GN:nusA] [FN:transcription termination] [OR:Bacillus subtilis] 111SPX0221 221 2882 98 294 220 1.70E-25 [LN:YLXR_BACSU] [AC:P32728][GN:YLXR] [OR:Bacillus subtilis] [DE:HYPOTHETICAL 10.4 KD PROTEIN INNUSA-INFB INTERGENIC REGION (ORF3)] [SP:P32728] 144 SPX0222 222 2883 100300 259 3.80E-31 [LN:YLXQ_ENTFC] [AC:P55768] [OR:Enterococcus faecium][SR:,Streptococcus faecium] [DE:PROBABLE RIBOSOMAL PROTEIN IN INFB5′REGION] [SP:P55768] 144 SPX0223 223 2884 165 495 NO-HIT 6 SPX0224 2242885 931 2793 2768 0 [GI:3947714] [LN:SAAJ3164] [AC:AJ003164][PN:initiation factor IF2] [GN:infB] [FN:translation initiation factor][OR:Streptococcus agalactiae] 142 SPX0225 225 2886 82 246 NO-HIT 6SPX0226 226 2887 117 351 478 2.00E-61 [GI:3947715] [LN:SAAJ3164][AC:AJ003164] [PN:ribosome binding factor A] [GN:rbfA] [FN:ribosomematuration] [OR:Streptococcus agalactiae] 136 SPX0227 227 2888 260 780217 3.30E-40 [LN:T35040] [AC:T35040] [PN:hypothetical protein SC4G2.05SC4G2.05] [GN:SC4G2.05] [OR:Streptomyces coelicolor] 110 SPX0228 2282889 84 252 NO-HIT 6 SPX0229 229 2890 74 222 NO-HIT 6 SPX0230 230 289165 195 202 2.70E-24 [LN:T30285] [AC:T30285] [PN:hypothetical protein][OR:Streptococcus pneumoniae] 79 SPX0231 231 2892 78 234 102 4.60E-08[LN:A69271] [AC:A69271] [PN:hypothetical protein AF0169][CL:Archaeoglobus fulgidus hypothetical protein AF0169][OR:Archaeoglobus fulgidus] 140 SPX0232 232 2893 445 1335 123 1.30E-41[LN:B69271] [AC:B69271] [PN:hypothetical protein AF0170][OR:Archaeoglobus fulgidus] 84 SPX0233 233 2894 85 255 NO-HIT 6 SPX0234234 2895 132 396 NO-HIT 6 SPX0235 235 2896 69 207 NO-HIT 6 SPX0236 2362897 150 450 NO-HIT 6 SPX0237 237 2898 186 558 148 2.10E-18[LN:YP20_BACLI] [AC:P05332] [GN:P20] [OR:Bacillus licheniformis][DE:HYPOTHETICAL P20 PROTEIN] [SP:P05332] 106 SPX0238 238 2899 321 963NO-HIT 6 SPX0239 239 2900 884 2652 1594 0 [LN:SYV_BACSU] [AC:Q05873][GN:VALS] [OR:Bacillus subtilis] [EC:6.1.1.9] [DE:VALYL-TRNA SYNTHETASE,(VALINE--TRNA LIGASE) (VALRS)] [SP:Q05873] 144 SPX0240 240 2901 252 756642 7.80E-85 [LN:B71947] [AC:B71947] [PN:hypothetical protein jhp0330][GN:jhp0330] [OR:Helicobacter pylori] [SR:strain J99, , strain J99][SR:strain J99, ] 145 SPX0241 241 2902 268 804 91 1.80E-05[LN:Y4LH_RHISN] [AC:P55548] [GN:Y4LH] [OR:Rhizobium sp] [SR:,strainNGR234] [DE:HYPOTHETICAL 22.4 KD PROTEIN Y4LH] [SP:P55548] 128 SPX0242242 2903 95 285 387 3.10E-49 [GI:1490399] [LN:SPPARCETP] [AC:Z67739][PN:DNA transposase] [OR:Streptococcus pneumoniae] 90 SPX0243 243 2904102 306 323 2.70E-40 [GI:1490399] [LN:SPPARCETP] [AC:Z67739] [PN:DNAtransposase] [OR:Streptococcus pneumoniae] 90 SPX0244 244 2905 91 273315 2.50E-39 [LN:A33595] [AC:A33595:A30868] [PN:probable transposase][CL:transposase IS3] [OR:Streptococcus agalactiae] 107 SPX0245 245 290692 276 135 3.80E-13 [LN:B30868] [AC:B30868] [PN:hypothetical protein 1][OR:Streptococcus agalactiae] 81 SPX0246 246 2907 422 1266 NO-HIT 6SPX0247 247 2908 399 1197 109 9.90E-10 [GI:6689196] [LN:SCE20][AC:AL136058] [PN:putative helicase] [GN:SCE20.37] [OR:Streptomycescoelicolor A3(2)] 109 SPX0248 248 2909 98 294 NO-HIT 6 SPX0249 249 2910280 840 489 2.30E-81 [LN:LICT_BACSU] [AC:P39805] [GN:LICT:N15A][OR:Bacillus subtilis] [DE:TRANSCRIPTION ANTITERMINATOR LICT][SP:P39805] 116 SPX0250 250 2911 613 1839 534 8.10E-147 [LN:PTBA_BACSU][AC:P40739:Q45661] [GN:BGLP:N17C] [OR:Bacillus subtilis] [EC:2.7.1.69][DE:ENZYME II, ABC COMPONENT), (EII-BGL)] [SP:P40739:Q45661] 149 SPX0251251 2912 472 1416 1046 3.70E-228 [LN:ABGA_CLOLO] [AC:Q46130] [GN:ABGA][OR:Clostridium longisporum] [EC:3.2.1.86][DE:6-PHOSPHO-BETA-GLUCOSIDASE,] [SP:Q46130] 127 SPX0252 252 2913 3491047 656 3.10E-156 [LN:SYFA_BACSU] [AC:P17921:P94539] [GN:PHES][OR:Bacillus subtilis] [EC:6.1.1.20] [DE:-TRNA LIGASE ALPHA CHAIN)(PHERS)] [SP:P17921:P94539] 139 SPX0253 253 2914 331 993 NO-HIT 6SPX0254 254 2915 170 510 333 1.80E-41 [LN:YPIP_LACDL] [AC:P46543][OR:Lactobacillus delbrueckii] [SR:,subsplactis] [DE:HYPOTHETICAL 19.8KD PROTEIN IN PEPI 3′REGION] [SP:P46543] 141 SPX0255 255 2916 801 2403312 2.20E-132 [LN:SYFB_SYNY3] [AC:P74296] [GN:PHET:SLL1553][OR:Synechocystis sp] [SR:,strain PCC 6803] [EC:6.1.1.20] [DE:TRNALIGASE BETA CHAIN) (PHERS)] [SP:P74296] 154 SPX0256 256 2917 296 888NO-HIT 6 SPX0257 257 2918 149 447 437 4.90E-55 [GI:517210] [LN:SPU11799][AC:U11799] [OR:Streptococcus pyogenes] 65 SPX0258 258 2919 89 267 2452.00E-28 [LN:Y659_HAEIN] [AC:P44030] [GN:HI0659] [OR:Haemophilusinfluenzae] [DE:HYPOTHETICAL PROTEIN HI0659] [SP:P44030] 112 SPX0259 2592920 99 297 NO-HIT 6 SPX0260 260 2921 750 2250 1309 6.60E-297[LN:C81326] [AC:C81326] [PN:5-methyltetrahydropteroyltriglutamate--homocystei methyltransferase, Cj1201 [imported]] [GN:metE:Cj1201][OR:Campylobacter jejuni] [EC:2.1.1.14] 175 SPX0261 261 2922 289 867 2613.90E-77 [LN:D81326] [AC:D81326] [PN:5,10-methylenetetrahydrofolatereductase, Cj1202 [imported]] [GN:metF:Cj1202] [OR:Campylobacter jejuni][EC:1.7.99.5] 147 SPX0262 262 2923 90 270 NO-HIT 6 SPX0263 263 2924 7382214 1323 3.80E-298 [LN:PNPA_BACSU] [AC:P50849] [GN:PNPA:COMR][OR:Bacillus subtilis] [EC:2.7.7.8] [DE:PHOSPHORYLASE) (PNPASE)(VEGETATIVE PROTEIN 15) (VEG15)] [SP:P50849] 151 SPX0264 264 2925 206618 493 1.20E-63 [GI:6899995] [LN:CST130879] [AC:AJ130879] [PN:serineacetyltransferase] [GN:cysE] [OR:Clostridium sticklandii] 110 SPX0265265 2926 295 885 113 3.80E-07 [LN:E69786] [AC:E69786][PN:ribosomal-protein-alanine N-acetyltransfer homolog ydiD] [GN:ydiD][CL:Escherichia coli ribosomal-protein-alanine N-acetyltransferase rimI][OR:Bacillus subtilis] 190 SPX0266 266 2927 152 456 NO-HIT 6 SPX0267 2672928 448 1344 570 9.00E-167 [GI:6899996] [LN:CST130879] [AC:AJ130879][PN:cysteinyl tRNA synthetase] [GN:cysRS] [OR:Clostridium sticklandii]112 SPX0268 268 2929 129 387 316 6.30E-39 [LN:C69742] [AC:C69742][PN:conserved hypothetical protein yazC] [GN:yazC] [OR:Bacillussubtilis] 97 SPX0269 269 2930 295 885 224 3.10E-30 [LN:LRPR_STREQ][AC:Q54087] [GN:LRP] [OR:Streptococcus equisimilis] [DE:LEUCINE RICHPROTEIN] [SP:Q54087] 105 SPX0270 270 2931 88 264 NO-HIT 6 SPX0271 2712932 200 600 NO-HIT 6 SPX0272 272 2933 52 156 87 3.30E-06 [LN:D75542][AC:D75542] [PN:hypothetical protein] [GN:DR0254] [OR:Deinococcusradiodurans] 90 SPX0273 273 2934 82 246 247 1.10E-29 [LN:F81737][AC:F81737] [PN:hypothetical protein TC0129 [imported]] [GN:TC0129][OR:Chlamydia muridarum:Chlamydia trachomatis MoPn] 131 SPX0274 274 293578 234 143 4.90E-15 [LN:F71245] [AC:F71245] [PN:hypothetical proteinPHS004] [GN:PHS004] [OR:Pyrococcus horikoshii] 95 SPX0275 275 2936 72216 NO-HIT 6 SPX0276 276 2937 63 189 68 2.40E-07 [LN:C64571] [AC:C64571][PN:hypothetical protein HP0411] [CL:Helicobacter pylori hypotheticalprotein HP0411] [OR:Helicobacter pylori] 134 SPX0277 277 2938 312 936194 2.60E-36 [GI:773349] [LN:BSU20445] [AC:U20445] [PN:BirA protein][GN:birA] [FN:biotin protein ligase, biotin operon repressor][OR:Bacillus subtilis] 142 SPX0278 278 2939 287 861 255 1.70E-56[LN:MSMR_STRMU] [AC:Q00753] [GN:MSMR] [OR:Streptococcus mutans] [DE:MSMOPERON REGULATORY PROTEIN] [SP:Q00753] 110 SPX0279 279 2940 721 21632528 0 [LN:AGAL_STRMU] [AC:P27756] [GN:AGA] [OR:Streptococcus mutans][EC:3.2.1.22] [DE:ALPHA-GALACTOSIDASE, (MELIBIASE)] [SP:P27756] 128SPX0280 280 2941 420 1260 1106 2.40E-180 [LN:MSME_STRMU] [AC:Q00749][GN:MSME] [OR:Streptococcus mutans] [DE:MULTIPLE SUGAR-BINDING PROTEINPRECURSOR] [SP:Q00749] 121 SPX0281 281 2942 82 246 NO-HIT 6 SPX0282 2822943 289 867 1188 1.40E-166 [LN:MSMF_STRMU] [AC:Q00750] [GN:MSMF][OR:Streptococcus mutans] [DE:MULTIPLE SUGAR-BINDING TRANSPORT SYSTEMPERMEASE PROTEIN MSMF] [SP:Q00750] 142 SPX0283 283 2944 278 834 11743.40E-164 [LN:MSMG_STRMU] [AC:Q00751] [GN:MSMG] [OR:Streptococcusmutans] [DE:MULTIPLE SUGAR-BINDING TRANSPORT SYSTEM PERMEASE PROTEINMSMG] [SP:Q00751] 142 SPX0284 284 2945 482 1446 2154 6.70E-294[LN:A27626] [AC:A27626] [PN:sucrose phosphorylase,] [CL:gtfA protein][OR:Streptococcus mutans] [EC:2.4.1.7] 110 SPX0285 285 2946 398 1194NO-HIT 6 SPX0286 286 2947 134 402 NO-HIT 6 SPX0287 287 2948 662 19863341 0 [LN:AMIA_STRPN] [AC:P18791:P18792] [GN:AMIA] [OR:Streptococcuspneumoniae] [DE:OLIGOPEPTIDE-BINDING PROTEIN AMIA PRECURSOR][SP:P18791:P18792] 142 SPX0288 288 2949 499 1497 2538 0 [LN:AMIC_STRPN][AC:P18793] [GN:AMIC] [OR:Streptococcus pneumoniae] [DE:OLIGOPEPTIDETRANSPORT PERMEASE PROTEIN AMIC] [SP:P18793] 129 SPX0289 289 2950 309927 1564 1.10E-217 [LN:AMID_STRPN] [AC:P18794] [GN:AMID][OR:Streptococcus pneumoniae] [DE:OLIGOPEPTIDE TRANSPORT PERMEASEPROTEIN AMID] [SP:P18794] 129 SPX0290 290 2951 356 1068 1806 2.10E-245[LN:AMIE_STRPN] [AC:P18765] [GN:AMIE] [OR:Streptococcus pneumoniae][DE:OLIGOPEPTIDE TRANSPORT ATP-BINDING PROTEIN AMIE] [SP:P18765] 132SPX0291 291 2952 113 339 NO-HIT 6 SPX0292 292 2953 309 927 15345.40E-208 [LN:AMIF_STRPN] [AC:P18766] [GN:AMIF] [OR:Streptococcuspneumoniae] [DE:OLIGOPEPTIDE TRANSPORT ATP-BINDING PROTEIN AMIF][SP:P18766] 132 SPX0293 293 2954 419 1257 2039 1.30E-284 [GI:2804700][LN:AF030361] [AC:AF030361] [PN:transposase] [OR:Streptococcuspneumoniae] 87 SPX0294 294 2955 96 288 274 1.10E-34 [GI:663279][LN:STRCOMAA] [AC:M36180:L15190] [PN:transposase] [OR:Streptococcuspneumoniae] [SR:Streptococcus pneumoniae (strain RX1) DNA] 138 SPX0295295 2956 173 519 840 6.50E-114 [GI:663278] [LN:STRCOMAA][AC:M36180:L15190] [PN:transposase] [OR:Streptococcus pneumoniae][SR:Streptococcus pneumoniae (strain RX1) DNA] 138 SPX0296 296 2957 237711 471 2.40E-60 [LN:TRER_BACSU] [AC:P39796] [GN:TRER] [OR:Bacillussubtilis] [DE:TREHALOSE OPERON TRANSCRIPTIONAL REPRESSOR] [SP:P39796]120 SPX0297 297 2958 656 1968 383 7.20E-135 [LN:PTTB_ECOLI] [AC:P36672][GN:TREB] [OR:Escherichia coli] [EC:2.7.1.69] [DE:(EC 2.7.1.69)(EII-TRE)] [SP:P36672] 114 SPX0298 298 2959 542 1626 1617 2.00E-272[GI:2208998] [LN:SSU35633] [AC:U35633] [PN:dextran glucosidase DexS][GN:dexS] [OR:Streptococcus suis] 102 SPX0299 299 2960 60 180 1252.30E-12 [LN:T30285] [AC:T30285] [PN:hypothetical protein][OR:Streptococcus pneumoniae] 79 SPX0300 300 2961 84 252 104 4.40E-09[GI:6899236] [LN:AE002123] [AC:AE002123:AF222894] [PN:conservedhypothetical] [GN:UU265] [OR:Ureaplasma urealyticum] 116 SPX0301 3012962 265 795 476 2.60E-84 [GI:2462097] [LN:BCBCTLGLR] [AC:Y10927][PN:glutamate racemase] [GN:bcglr] [OR:Bacillus cereus] 95 SPX0302 3022963 297 891 273 9.10E-35 [LN:C69986] [AC:C69986] [PN:conservedhypothetical protein ysnA] [GN:ysnA] [CL:Methanococcus jannaschiiconserved hypothetical protein MJ0226] [OR:Bacillus subtilis] 165SPX0303 303 2964 74 222 158 1.60E-15 [LN:YGGV_ECOLI] [AC:P52061][GN:YGGV] [OR:Escherichia coli] [DE:HYPOTHETICAL 21.0 KD PROTEIN INGSHB-ANSB INTERGENIC REGION (O197)] [SP:P52061] 143 SPX0304 304 2965 174522 229 8.10E-27 [LN:YSNB_BACSU] [AC:P94559] [GN:YSNB] [OR:Bacillussubtilis] [DE:HYPOTHETICAL 19.2 KD PROTEIN IN RPH-ILVB INTERGENICREGION] [SP:P94559] 136 SPX0305 305 2966 154 462 75 8.30E-08 [LN:A69866][AC:A69866] [PN:hypothetical protein ykuL] [GN:ykuL] [CL:Bacillussubtilis hypothetical protein ykuL] [OR:Bacillus subtilis] 136 SPX0306306 2967 247 741 61 0.0006 [LN:A75153] [AC:A75153][PN:integrase/recombinase xerd PAB0255] [GN:xerD-like:PAB0255][CL:probable site-specific integrase/recombinase XerC] [OR:Pyrococcusabyssi] 164 SPX0307 307 2968 243 729 233 1.60E-40 [LN:YPUG_BACSU][AC:P35154] [GN:YPUG] [OR:Bacillus subtilis] [DE:HYPOTHETICAL 29.6 KDPROTEIN IN RIBT-DACB INTERGENIC REGION (ORFX7)] [SP:P35154] 145 SPX0308308 2969 190 570 216 2.00E-28 [LN:Y214_MYCPN] [AC:P75477] [OR:Mycoplasmapneumoniae] [DE:HYPOTHETICAL PROTEIN MG214 HOMOLOG] [SP:P75477] 106SPX0309 309 2970 241 723 660 5.60E-86 [LN:RLUB_BACSU] [AC:P35159][GN:RLUB] [OR:Bacillus subtilis] [EC:4.2.1.70] [DE:(PSEUDOURIDYLATESYNTHASE) (URACIL HYDROLYASE)] [SP:P35159] 138 SPX0310 310 2971 81 243166 1.10E-32 [LN:G72251] [AC:G72251] [PN:conserved hypothetical protein][GN:TM1462] [CL:conserved hypothetical protein HI1000] [OR:Thermotogamaritima] 139 SPX0311 311 2972 175 525 NO-HIT 6 SPX0312 312 2973 322 966218 2.70E-57 [LN:E69763] [AC:E69763] [PN:probable ferrichrome ABCtransporter yclQ] [GN:yclQ] [CL:iron(III) dicitrate transport protein][OR:Bacillus subtilis] 146 SPX0313 313 2974 251 753 702 2.90E-92[LN:D69763] [AC:D69763] [PN:ferrichrome ABC transporter (ATP-binding p)homolog yclP] [GN:yclP] [CL:unassigned ATP-binding cassetteproteins:ATP-binding cassette homology] [OR:Bacillus subtilis] 194SPX0314 314 2975 67 201 89 6.60E-07 [LN:G72510] [AC:G72510][PN:hypothetical protein APE2061] [GN:APE2061] [OR:Aeropyrum pernix] 92SPX0315 315 2976 319 957 474 8.60E-64 [LN:C69763] [AC:C69763][PN:ferrichrome ABC transporter (permease) homolog yclO] [GN:yclO][CL:ferrichrome ABC transporter] [OR:Bacillus subtilis] 146 SPX0316 3162977 320 960 625 2.80E-84 [LN:B69763] [AC:B69763] [PN:ferrichrome ABCtransporter (permease) homolog yclN] [GN:yclN] [CL:vitamin B12 transportprotein btuC] [OR:Bacillus subtilis] 153 SPX0317 317 2978 136 408 2883.50E-36 [GI:6707010] [LN:AF109295] [AC:AF109295:AF022796] [PN:GalE][GN:galE] [OR:Staphylococcus carnosus] 98 SPX0318 318 2979 81 243 1646.20E-18 [GI:3703059] [LN:AF082009] [AC:AF082009][PN:UDP-galactose-4-epimerase] [GN:galE] [OR:Lactococcus lactis] 105SPX0319 319 2980 354 1062 388 8.30E-143 [LN:PEPA_LACLC] [AC:Q48677][GN:PEPA] [OR:Lactococcus lactis] [SR:,subspcremoris:Streptococcuscremoris] [EC:3.4.11.7] [DE:GLUTAMYL-AMINOPEPTIDASE,] [SP:Q48677] 162SPX0320 320 2981 99 297 NO-HIT 6 SPX0321 321 2982 63 189 NO-HIT 6SPX0322 322 2983 148 444 87 0.00059 [GI:2791904] [LN:SSK3MECA1][AC:Y13052] [GN:ORF145] [OR:Staphylococcus sciuri] 78 SPX0323 323 2984255 765 NO-HIT 6 SPX0324 324 2985 243 729 1211 8.40E-163 [GI:5579394][LN:AF162655] [AC:AF162655] [PN:choline transporter] [GN:proV][FN:ATPase] [OR:Streptococcus pneumoniae] 117 SPX0325 325 2986 29 87NO-HIT 6 SPX0326 326 2987 311 933 1434 2.40E-200 [LN:T44634] [AC:T44634][PN:choline transporter [imported]] [GN:proWX] [OR:Streptococcuspneumoniae] 100 SPX0327 327 2988 210 630 1042 3.30E-137 [LN:T44634][AC:T44634] [PN:choline transporter [imported]] [GN:proWX][OR:Streptococcus pneumoniae] 100 SPX0328 328 2989 270 810 125 1.90E-15[LN:YA7B_HAEIN] [AC:Q57425:P96338] [GN:HI1077.1] [OR:Haemophilusinfluenzae] [DE:HYPOTHETICAL PROTEIN HI1077.1] [SP:Q57425:P96338] 130SPX0329 329 2990 179 537 150 8.10E-17 [GI:5881867] [LN:SC5G9][AC:AL117385] [PN:putative tetR-family transcriptional regulator][GN:SC5G9.19c] [OR:Streptomyces coelicolor A3(2)] 139 SPX0330 330 2991300 900 202 5.60E-39 [GI:1944409] [LN:D87026] [AC:D87026:D28136][PN:membrane protein] [OR:Bacillus stearothermophilus] [SR:Bacillusstearothermophilus (strain:TRBE14) DNA] 151 SPX0331 331 2992 118 354 2823.60E-34 [LN:B69970] [AC:B69970] [PN:transcription regulator MerR familyhomolog yraB] [GN:yraB] [CL:transcription repressor glnR] [OR:Bacillussubtilis] 144 SPX0332 332 2993 346 1038 403 3.80E-82 [LN:T44975][AC:T44975] [PN:dehydrogenase [imported]] [CL:alcoholdehydrogenase:long-chain alcohol dehydrogenase homology] [OR:Haloferaxvolcanii] 146 SPX0333 333 2994 336 1008 729 4.00E-144 [GI:4097439][LN:STU61402] [AC:U61402] [PN:GalR] [GN:galR] [OR:Streptococcusthermophilus] 90 SPX0334 334 2995 393 1179 1674 3.10E-227 [GI:4097440][LN:STU61402] [AC:U61402] [PN:galactokinase] [GN:galK] [FN:galactosemetabolism] [OR:Streptococcus thermophilus] 125 SPX0335 335 2996 4941482 1612 1.90E-230 [GI:4097441] [LN:STU61402] [AC:U61402] [PN:gal-1-Puridylyltransferase] [GN:galT] [FN:galactose metabolism][OR:Streptococcus thermophilus] 139 SPX0336 336 2997 135 405 4671.10E-60 [GI:1196924] [LN:STRDPN2A] [AC:M14339] [PN:unknown][OR:Streptococcus pneumoniae] 81 SPX0337 337 2998 296 888 1461 6.00E-199[LN:MT21_STRPN] [AC:P04043] [GN:DPNM] [OR:Streptococcus pneumoniae][EC:2.1.1.72] [DE:METHYLTRANSFERASE DPNII 1) (M.DPNII 1)] [SP:P04043]137 SPX0338 338 2999 257 771 1366 2.60E-183 [LN:MT22_STRPN] [AC:P09358][GN:DPNA] [OR:Streptococcus pneumoniae] [EC:2.1.1.72][DE:METHYLTRANSFERASE DPNII 2) (M.DPNII 2)] [SP:P09358] 137 SPX0339 3393000 289 867 1492 5.50E-202 [LN:T2D2_STRPN] [AC:P09357] [GN:DPNB][OR:Streptococcus pneumoniae] [EC:3.1.21.4] [DE:(R.DPNII)] [SP:P09357]108 SPX0340 340 3001 119 357 462 1.20E-61 [GI:6978345] [LN:STRDPN2A][AC:M14339] [PN:unknown] [OR:Streptococcus pneumoniae] 81 SPX0341 3413002 283 849 436 8.70E-87 [LN:YUNK_BACSU] [AC:O32140] [GN:YUNK][OR:Bacillus subtilis] [DE:HYPOTHETICAL 44.9 KD PROTEIN IN HOM-MRGAINTERGENIC REGION] [SP:O32140] 136 SPX0342 342 3003 194 582 7863.40E-105 [GI:7160242] [LN:SPN272465] [AC:AJ272465] [PN:xanthinephosphoribosyltransferase] [GN:xpt] [OR:Streptococcus pneumoniae] 120SPX0343 343 3004 58 174 79 7.70E-11 [LN:T30285] [AC:T30285][PN:hypothetical protein] [OR:Streptococcus pneumoniae] 79 SPX0344 3443005 80 240 113 5.90E-10 [LN:C75408] [AC:C75408] [PN:hypotheticalprotein] [GN:DR1341] [OR:Deinococcus radiodurans] 90 SPX0345 345 3006276 828 1432 8.60E-192 [LN:EXOA_STRPN] [AC:P21998] [GN:EXOA][OR:Streptococcus pneumoniae] [EC:3.1.11.2] [DE:EXODEOXYRIBONUCLEASE,][SP:P21998] 122 SPX0346 346 3007 76 228 NO-HIT 6 SPX0347 347 3008 90 270NO-HIT 6 SPX0348 348 3009 177 531 132 9.60E-19 [LN:F69972] [AC:F69972][PN:probable membrane protein yrbG] [GN:yrbG] [CL:probable membraneprotein ycaP] [OR:Bacillus subtilis] 128 SPX0349 349 3010 79 237 1295.90E-21 [GI:1914870] [LN:SPZ82001] [AC:Z82001] [PN:unknown][OR:Streptococcus pneumoniae] 81 SPX0350 350 3011 582 1746 685 1.90E-170[LN:A69829] [AC:A69829] [PN:ABC transporter (ATP-binding protein)homolog yheI] [GN:yheI] [CL:unassigned ATP-binding cassetteproteins:ATP-binding cassette homology] [OR:Bacillus subtilis] 188SPX0351 351 3012 294 882 364 6.80E-49 [LN:H69828] [AC:H69828] [PN:ABCtransporter (ATP-binding protein) homolog yheH] [GN:yheH] [CL:unassignedATP-binding cassette proteins:ATP-binding cassette homology][OR:Bacillus subtilis] 188 SPX0352 352 3013 69 207 82 0.00022[LN:H69828] [AC:H69828] [PN:ABC transporter (ATP-binding protein)homolog yheH] [GN:yheH] [CL:unassigned ATP-binding cassetteproteins:ATP-binding cassette homology] [OR:Bacillus subtilis] 188SPX0353 353 3014 264 792 383 3.90E-79 [LN:H69828] [AC:H69828] [PN:ABCtransporter (ATP-binding protein) homolog yheH] [GN:yheH] [CL:unassignedATP-binding cassette proteins:ATP-binding cassette homology][OR:Bacillus subtilis] 188 SPX0354 354 3015 232 696 632 1.10E-83[GI:6601354] [LN:AF164515] [AC:AF164515] [PN:putativeglycosyltransferase Cps7F] [GN:cps7F] [OR:Streptococcus suis] 115SPX0355 355 3016 409 1227 973 4.70E-214 [GI:6601355] [LN:AF164515][AC:AF164515] [PN:Cps7G] [GN:cps7G] [OR:Streptococcus suis] 86 SPX0356356 3017 63 189 NO-HIT 6 SPX0357 357 3018 89 267 NO-HIT 6 SPX0358 3583019 709 2127 107 4.60E-08 [GI:2952545] [LN:AF051898] [AC:AF051898][PN:coronin binding protein] [GN:DB10] [OR:Dictyostelium discoideum] 109SPX0359 359 3020 82 246 NO-HIT 6 SPX0360 360 3021 69 207 NO-HIT 6SPX0361 361 3022 95 285 NO-HIT 6 SPX0362 362 3023 96 288 289 6.60E-34[GI:43589] [LN:HILIC3] [AC:X57315] [PN:UDP-galactose-4-epimerase][GN:galE] [OR:Haemophilus influenzae] 103 SPX0363 363 3024 66 198 NO-HIT6 SPX0364 364 3025 220 660 NO-HIT 6 SPX0365 365 3026 356 1068 2862.20E-30 [LN:Y4FP_RHISN] [AC:P55454] [GN:Y4FP] [OR:Rhizobium sp][SR:,strain NGR234] [DE:PROBABLE ABC TRANSPORTER PERIPLASMIC BINDINGPROTEIN Y4FP PRECURSOR] [SP:P55454] 162 SPX0366 366 3027 337 1011 3953.30E-90 [LN:A70180] [AC:A70180] [PN:spermidine/putrescine ABCtransporter, ATP-binding protein (potA) homolog] [CL:unassignedATP-binding cassette proteins:ATP-binding cassette homology][OR:Borrelia burgdorferi] [SR:, Lyme disease spirochete] 237 SPX0367 3673028 564 1692 433 1.50E-93 [LN:Y4FN_RHISN] [AC:P55452] [GN:Y4FN][OR:Rhizobium sp] [SR:,strain NGR234] [DE:PROBABLE ABC TRANSPORTERPERMEASE PROTEIN Y4FN] [SP:P55452] 141 SPX0368 368 3029 237 711 1924.80E-28 [LN:Y647_HAEIN] [AC:Q57424:O05028] [GN:HI0647] [OR:Haemophilusinfluenzae] [DE:HYPOTHETICAL PROTEIN HI0647] [SP:Q57424:O05028] 126SPX0369 369 3030 103 309 NO-HIT 6 SPX0370 370 3031 334 1002 144 3.70E-25[LN:CCPA_BACME] [AC:P46828] [GN:CCPA] [OR:Bacillus megaterium][DE:GLUCOSE-RESISTANCE AMYLASE REGULATOR (CATABOLITE CONTROL PROTEIN)][SP:P46828] 145 SPX0371 371 3032 66 198 NO-HIT 6 SPX0372 372 3033 69 207NO-HIT 6 SPX0373 373 3034 488 1464 1100 2.50E-173 [LN:TRPE_LACLA][AC:Q02001] [GN:TRPE] [OR:Lactococcus lactis][SR:,subsplactis:Streptococcus lactis] [EC:4.1.3.27] [DE:ANTHRANILATESYNTHASE COMPONENT I,] [SP:Q02001] 168 SPX0374 374 3035 67 201 1086.30E-10 [LN:C72489] [AC:C72489] [PN:hypothetical protein APE2554][GN:APE2554] [OR:Aeropyrum pernix] 92 SPX0375 375 3036 189 567 4408.80E-75 [LN:TRPG_LACLA] [AC:Q02003] [GN:TRPG] [OR:Lactococcus lactis][SR:,subsplactis:Streptococcus lactis] [EC:4.1.3.27] [DE:TRANSFERASE)][SP:Q02003] 146 SPX0376 376 3037 335 1005 1008 9.70E-134 [LN:TRPD_LACLA][AC:Q02000] [GN:TRPD] [OR:Lactococcus lactis][SR:,subsplactis:Streptococcus lactis] [EC:2.4.2.18] [DE:ANTHRANILATEPHOSPHORIBOSYLTRANSFERASE,] [SP:Q02000] 173 SPX0377 377 3038 256 768 4466.20E-107 [LN:TRPC_LACLA] [AC:Q01999] [GN:TRPC] [OR:Lactococcus lactis][SR:,subsplactis:Streptococcus lactis] [EC:4.1.1.48][DE:INDOLE-3-GLYCEROL PHOSPHATE SYNTHASE, (IGPS)] [SP:Q01999] 178SPX0378 378 3039 210 630 225 3.50E-49 [LN:TRPF_LACLA] [AC:Q02002][GN:TRPF] [OR:Lactococcus lactis] [SR:,subsplactis:Streptococcus lactis][EC:5.3.1.24] [DE:N-(5′-PHOSPHORIBOSYL)ANTHRANILATE ISOMERASE, (PRAI)][SP:Q02002] 185 SPX0379 379 3040 408 1224 930 9.00E-225 [LN:TRPB_LACLA][AC:Q01998] [GN:TRPB] [OR:Lactococcus lactis][SR:,subsplactis:Streptococcus lactis] [EC:4.2.1.20] [DE:TRYPTOPHANSYNTHASE BETA CHAIN,] [SP:Q01998] 165 SPX0380 380 3041 278 834 11375.00E-153 [GI:5231181] [LN:AF157817] [AC:AF157817] [PN:tryptophansynthase alpha chain] [GN:trpA] [OR:Streptococcus pneumoniae] 117SPX0381 381 3042 68 204 NO-HIT 6 SPX0382 382 3043 244 732 NO-HIT 6SPX0383 383 3044 384 1152 92 2.70E-13 [LN:H70940] [AC:H70940][PN:probable helix-turn-helix motif at aa 18-39] [GN:Rv2017][OR:Mycobacterium tuberculosis] 116 SPX0384 384 3045 220 660 1091.00E-14 [LN:B72220] [AC:B72220] [PN:type IV prepilin peptidase][GN:TM1696] [CL:type IV prepilin peptidase] [OR:Thermotoga maritima] 124SPX0385 385 3046 149 447 92 0.00011 [LN:E72312] [AC:E72312][PN:conserved hypothetical protein] [GN:TM0968] [CL:Escherichia coliribosomal-protein-alanine N-acetyltransferase rimJ] [OR:Thermotogamaritima] 169 SPX0386 386 3047 104 312 138 1.30E-12 [GI:6332767][LN:AB033763] [AC:AB033763:AB014419:AB014429:AB014439] [PN:hypotheticalprotein] [OR:Staphylococcus aureus] [SR:Staphylococcus aureus(strain:NCTC10442) DNA, clone_lib:Lambda das] 194 SPX0387 387 3048 68204 98 8.10E-08 [GI:2772940] [LN:AF034574] [AC:AF034574] [PN:putativecruciform DNA binding protein] [GN:Gv1] [OR:Glomus versiforme] 116SPX0388 388 3049 203 609 515 8.70E-64 [GI:727436] [LN:LLU23376][AC:U23376] [OR:Lactococcus lactis] 61 SPX0389 389 3050 191 573 NO-HIT 6SPX0390 390 3051 513 1539 193 6.90E-35 [GI:6782400] [LN:STC133440][AC:AJ133440] [PN:multigene regulator protein Mgc, putative] [GN:mgc][FN:gene regulatory function, putative] [OR:Streptococcus dysgalactiae]171 SPX0391 391 3052 334 1002 185 3.80E-46 [LN:SCRR_STRMU] [AC:Q54430][GN:SCRR] [OR:Streptococcus mutans] [DE:SUCROSE OPERON REPRESSOR (SCROPERON REGULATORY PROTEIN)] [SP:Q54430] 137 SPX0392 392 3053 315 945 3762.50E-89 [LN:A69653] [AC:A69653] [PN:transmembrane lipoprotein lplB][GN:lplB] [CL:inner membrane protein ugpA] [OR:Bacillus subtilis] 125SPX0393 393 3054 306 918 450 1.20E-73 [LN:LPLC_BACSU] [AC:P39129][GN:LPLC] [OR:Bacillus subtilis] [DE:LPLC PROTEIN] [SP:P39129] 90SPX0394 394 3055 539 1617 167 2.90E-15 [GI:4056657] [LN:AF098273][AC:AF098273] [PN:peripheral protein] [GN:glucuronic acid catabolismoperon] [OR:Bacillus stearothermophilus] 136 SPX0395 395 3056 141 423NO-HIT 6 SPX0396 396 3057 440 1320 305 2.30E-76 [LN:RAFD_ECOLI][AC:P16553] [GN:RAFD] [OR:Escherichia coli] [EC:3.2.1.26] [DE:RAFFINOSEINVERTASE, (INVERTASE)] [SP:P16553] 125 SPX0397 397 3058 424 1272 7227.10E-167 [LN:D69981] [AC:D69981] [PN:conserved hypothetical proteinyrvN] [GN:yrvN] [CL:Haemophilus influenzae conserved hypotheticalprotein HI1590] [OR:Bacillus subtilis] 163 SPX0398 398 3059 74 222NO-HIT 6 SPX0399 399 3060 60 180 NO-HIT 6 SPX0400 400 3061 84 252 NO-HIT6 SPX0401 401 3062 151 453 92 4.90E-09 [LN:T13557] [AC:T13557][PN:hypothetical protein 17] [CL:Archaeoglobus fulgidus conservedhypothetical protein AF1072] [OR:Bacillus phage phi-105] 146 SPX0402 4023063 157 471 NO-HIT 6 SPX0403 403 3064 363 1089 NO-HIT 6 SPX0404 4043065 345 1035 130 8.00E-15 [GI:758793] [LN:ECU23723] [AC:U23723][FN:unknown] [OR:Escherichia coli] 72 SPX0405 405 3066 748 2244 680.00048 [GI:758794] [LN:ECU23723] [AC:U23723] [FN:unknown][OR:Escherichia coli] 72 SPX0406 406 3067 340 1020 NO-HIT 6 SPX0407 4073068 317 951 395 1.40E-81 [LN:T43740] [AC:T43740] [PN:probable ribosomalprotein L11 methyltransferase, [imported]:hypothetical protein 35][CL:ribosomal protein L11 methyltransferase:bioC homology] [OR:Listeriamonocytogenes] [EC:2.1.1.-] 215 SPX0408 408 3069 248 744 461 1.90E-64[LN:T43741] [AC:T43741] [PN:conserved hypothetical protein orf29[imported]] [OR:Listeria monocytogenes] 104 SPX0409 409 3070 599 1797300 2.10E-57 [LN:PEPF_BACSU] [AC:O31605] [GN:YJBG] [OR:Bacillussubtilis] [EC:3.4.24.-] [DE:OLIGOENDOPEPTIDASE F HOMOLOG,] [SP:O31605]123 SPX0410 410 3071 226 678 312 1.80E-58 [LN:D69780] [AC:D69780][PN:hypothetical protein ydfF] [GN:ydfF] [OR:Bacillus subtilis] 87SPX0411 411 3072 217 651 394 1.40E-54 [LN:G69803] [AC:G69803] [PN:ABCtransporter (ATP-binding protein) homolog yfiL] [GN:yfiL] [CL:unassignedATP-binding cassette proteins:ATP-binding cassette homology][OR:Bacillus subtilis] 188 SPX0412 412 3073 255 765 346 4.20E-44[LN:NODJ_RHILV] [AC:P06755] [GN:NODJ] [OR:Rhizobium leguminosarum][SR:,biovar viciae] [DE:NODULATION PROTEIN J] [SP:P06755] 126 SPX0413413 3074 264 792 NO-HIT 6 SPX0414 414 3075 210 630 257 3.90E-39[LN:A69428] [AC:A69428] [PN:glycerol uptake facilitator, MIP channel(glpF) homolog] [CL:nodulin-26] [OR:Archaeoglobus fulgidus] 130 SPX0415415 3076 60 180 NO-HIT 6 SPX0416 416 3077 191 573 467 1.10E-60[LN:D69868] [AC:D69868] [PN:conserved hypothetical protein ykvM][GN:ykvM] [CL:hypothetical protein ykvM] [OR:Bacillus subtilis] 128SPX0417 417 3078 105 315 193 1.80E-43 [GI:5640117] [LN:LMO133006][AC:AJ133006] [PN:thioredoxin] [GN:trxA] [FN:thiol:disulfideinterchange] [OR:Listeria monocytogenes] 129 SPX0418 418 3079 101 303NO-HIT 6 SPX0419 419 3080 67 201 NO-HIT 6 SPX0420 420 3081 75 225 NO-HIT6 SPX0421 421 3082 318 954 433 2.70E-56 [LN:YQJA_BACSU] [AC:P54538][GN:YQJA] [OR:Bacillus subtilis] [DE:HYPOTHETICAL 37.1 KD PROTEIN INBMRU-ANSR INTERGENIC REGION] [SP:P54538] 137 SPX0422 422 3083 287 861745 1.50E-100 [LN:YGJU_HAEIN] [AC:P45246] [GN:HI1545] [OR:Haemophilusinfluenzae] [DE:HYPOTHETICAL SYMPORTER HI1545] [SP:P45246] 114 SPX0423423 3084 75 225 153 4.00E-15 [LN:YGJU_ECOLI] [AC:P42602] [GN:YGJU][OR:Escherichia coli] [DE:HYPOTHETICAL 43.5 KD PROTEIN IN EBGC-UXAAINTERGENIC REGION (O414)] [SP:P42602] 143 SPX0424 424 3085 140 420 1632.90E-17 [GI:2828366] [LN:AB010789] [AC:AB010789] [OR:Lactococcuslactis] [SR:Lactococcus lactis (sub_species:lactis, strain:01-7) DNA]128 SPX0425 425 3086 66 198 102 1.80E-07 [LN:A69867] [AC:A69867][PN:conserved hypothetical protein ykuT] [GN:ykuT] [CL:Escherichia colihypothetical 30.9K protein (sbm-fba intergenic region)] [OR:Bacillussubtilis] 174 SPX0426 426 3087 59 177 NO-HIT 6 SPX0427 427 3088 303 909270 1.70E-35 [GI:5123526] [LN:AF036485][AC:AF036485:AF036486:AF036487:U93364] [PN:hypothetical protein][OR:Plasmid pNZ4000] 112 SPX0428 428 3089 176 528 326 9.70E-41[LN:YQEG_BACSU] [AC:P54452] [GN:YQEG] [OR:Bacillus subtilis][DE:HYPOTHETICAL 20.1 KD PROTEIN IN NUCB-AROD INTERGENIC REGION][SP:P54452] 137 SPX0429 429 3090 369 1107 1037 1.30E-164 [LN:YQEH_BACSU][AC:P54453] [GN:YQEH] [OR:Bacillus subtilis] [DE:HYPOTHETICAL 41.0 KDPROTEIN IN NUCB-AROD INTERGENIC REGION] [SP:P54453] 137 SPX0430 430 3091104 312 211 5.20E-24 [LN:YQEI_BACSU] [AC:P54454] [GN:YQEI] [OR:Bacillussubtilis] [DE:HYPOTHETICAL 10.8 KD PROTEIN IN AROD-COMER INTERGENICREGION] [SP:P54454] 138 SPX0431 431 3092 205 615 491 1.30E-63[LN:YQEJ_BACSU] [AC:P54455] [GN:YQEJ] [OR:Bacillus subtilis][DE:HYPOTHETICAL 22.2 KD PROTEIN IN AROD-COMER INTERGENIC REGION][SP:P54455] 138 SPX0432 432 3093 198 594 375 2.90E-47 [LN:YQEK_BACSU][AC:P54456] [GN:YQEK] [OR:Bacillus subtilis] [DE:HYPOTHETICAL 21.3 KDPROTEIN IN AROD-COMER INTERGENIC REGION] [SP:P54456] 138 SPX0433 4333094 167 501 110 4.90E-10 [GI:7160132] [LN:SC5C11] [AC:AL158060][PN:putative isochorismatase.] [GN:SC5C11.12] [OR:Streptomycescoelicolor A3(2)] 119 SPX0434 434 3095 118 354 267 7.00E-32[LN:YQEL_BACSU] [AC:P54457] [GN:YQEL] [OR:Bacillus subtilis][DE:HYPOTHETICAL 13.3 KD PROTEIN IN AROD-COMER INTERGENIC REGION][SP:P54457] 138 SPX0435 435 3096 247 741 287 4.60E-55 [LN:YQEM_BACSU][AC:P54458] [GN:YQEM] [OR:Bacillus subtilis] [DE:HYPOTHETICAL 28.3 KDPROTEIN IN AROD-COMER INTERGENIC REGION] [SP:P54458] 138 SPX0436 4363097 188 564 NO-HIT 6 SPX0437 437 3098 366 1098 222 9.30E-38 [LN:B69875][AC:B69875] [PN:conserved hypothetical protein ylbM] [GN:ylbM][OR:Bacillus subtilis] 97 SPX0438 438 3099 63 189 NO-HIT 6 SPX0439 4393100 916 2748 86 1.00E-10 [GI:1890605] [LN:RMEXPGNS] [AC:Z79692][PN:ORF25] [OR:Sinorhizobium meliloti] 77 SPX0440 440 3101 537 1611 15472.30E-211 [GI:6984124] [LN:AF228345] [AC:AF228345] [PN:unknown][OR:Listeria monocytogenes] 81 SPX0441 441 3102 209 627 614 1.40E-80[LN:B69878] [AC:B69878] [PN:guanylate kinase homolog yloD] [GN:yloD][CL:guanylate kinase:guanylate kinase homology] [OR:Bacillus subtilis]139 SPX0442 442 3103 105 315 91 1.00E-09 [LN:C69878] [AC:C69878][PN:hypothetical protein yloH] [GN:yloH] [OR:Bacillus subtilis] 87SPX0443 443 3104 799 2397 953 2.70E-237 [LN:PRIA_BACSU][AC:P94461:O34941] [GN:PRIA] [OR:Bacillus subtilis] [DE:PRIMOSOMALPROTEIN N′(REPLICATION FACTOR Y)] [SP:P94461:O34941] 136 SPX0444 4443105 312 936 434 1.70E-64 [GI:1772500] [LN:BSPRIADFS] [AC:Y10304][PN:Met-tRNAi formyl transferase] [GN:fmt] [OR:Bacillus subtilis] 105SPX0445 445 3106 176 528 248 1.40E-39 [GI:1772501] [LN:BSPRIADFS][AC:Y10304] [GN:sun] [OR:Bacillus subtilis] 71 SPX0446 446 3107 139 417130 1.30E-09 [GI:4210751] [LN:LLA132604] [AC:AJ132604] [PN:sunL protein][GN:sunL] [OR:Lactococcus lactis] 93 SPX0447 447 3108 233 699 6062.70E-80 [GI:4210751] [LN:LLA132604] [AC:AJ132604] [PN:sunL protein][GN:sunL] [OR:Lactococcus lactis] 93 SPX0448 448 3109 247 741 3711.50E-85 [GI:4210752] [LN:LLA132604] [AC:AJ132604] [PN:pppL protein][GN:pppL] [FN:putative phosphoprotein phosphatase] [OR:Lactococcuslactis] 134 SPX0449 449 3110 660 1980 985 1.70E-128 [GI:4210753][LN:LLA132604] [AC:AJ132604] [PN:hypothetical protein] [OR:Lactococcuslactis] 91 SPX0450 450 3111 68 204 NO-HIT 6 SPX0451 451 3112 74 222NO-HIT 6 SPX0452 452 3113 170 510 125 1.80E-09 [LN:YJJP_ECOLI][AC:P39402] [GN:YJJP] [OR:Escherichia coli] [DE:HYPOTHETICAL 30.5 KDPROTEIN IN DNAT-BGLJ INTERGENIC REGION (F277)] [SP:P39402] 143 SPX0453453 3114 112 336 94 4.60E-07 [LN:G81321] [AC:G81321] [PN:probableintegral membrane protein Cj1165c [imported]] [GN:Cj1165c][OR:Campylobacter jejuni] 121 SPX0454 454 3115 67 201 217 3.80E-24[LN:S52544] [AC:S52544] [PN:ISL2 protein] [OR:Lactobacillus helveticus]71 SPX0455 455 3116 130 390 362 7.00E-46 [LN:S52544] [AC:S52544][PN:ISL2 protein] [OR:Lactobacillus helveticus] 71 SPX0456 456 3117 96288 NO-HIT 6 SPX0457 457 3118 391 1173 775 1.30E-101 [GI:4096796][LN:SCU40157] [AC:U40157] [OR:Staphylococcus carnosus] 67 SPX0458 4583119 425 1275 354 8.70E-92 [LN:MVAA_PSEMV] [AC:P13702] [GN:MVAA][OR:Pseudomonas mevalonii] [EC:1.1.1.88] [DE:REDUCTASE)] [SP:P13702] 106SPX0459 459 3120 322 966 1108 1.00E-150 [LN:SCRR_STRMU] [AC:Q54430][GN:SCRR] [OR:Streptococcus mutans] [DE:SUCROSE OPERON REPRESSOR (SCROPERON REGULATORY PROTEIN)] [SP:Q54430] 137 SPX0460 460 3121 485 14551691 3.60E-229 [LN:S68598] [AC:S68598] [PN:sucrose-6-phosphate hydrolaseScrB] [GN:scrB] [CL:sucrose-6-phosphate hydrolase] [OR:Streptococcussobrinus] [SR:strain 6715, , strain 6715] [SR:strain 6715, ] 189 SPX0461461 3122 77 231 NO-HIT 6 SPX0462 462 3123 66 198 NO-HIT 6 SPX0463 4633124 628 1884 717 6.70E-255 [LN:S68599] [AC:S68599][PN:phosphotransferase system enzyme II,,sucrose-specific:sucrose-specific enzyme II:sucrose-specific enzyme II][GN:scrA] [OR:Streptococcus sobrinus] 177 SPX0464 464 3125 296 888 7013.80E-158 [LN:SCRK_STRMU] [AC:Q07211] [GN:SCRK] [OR:Streptococcusmutans] [EC:2.7.1.4] [DE:FRUCTOKINASE,] [SP:Q07211] 109 SPX0465 465 312671 213 NO-HIT 6 SPX0466 466 3127 200 600 103 2.90E-07 [LN:YDJZ_ECOLI][AC:P76221] [GN:YDJZ] [OR:Escherichia coli] [DE:HYPOTHETICAL 26.2 KDPROTEIN IN XTHA-GDHA INTERGENIC REGION] [SP:P76221] 136 SPX0467 467 312875 225 200 1.30E-21 [GI:517210] [LN:SPU11799] [AC:U11799][OR:Streptococcus pyogenes] 65 SPX0468 468 3129 84 252 NO-HIT 6 SPX0469469 3130 76 228 187 3.50E-21 [LN:T30285] [AC:T30285] [PN:hypotheticalprotein] [OR:Streptococcus pneumoniae] 79 SPX0470 470 3131 298 894 4601.20E-78 [GI:3688825] [LN:AF084104] [AC:AF084104] [PN:NatA] [GN:natA][OR:Bacillus firmus] 81 SPX0471 471 3132 400 1200 200 4.70E-36[GI:1150487] [LN:LSLASAMPT] [AC:Z54312] [PN:unknown] [GN:orf414][OR:Lactobacillus sakei] 89 SPX0472 472 3133 56 168 NO-HIT 6 SPX0473 4733134 283 849 NO-HIT 6 SPX0474 474 3135 241 723 460 1.50E-58 [LN:G71842][AC:G71842] [PN:probable ABC transporter, ATP-binding protein][GN:jhp1141] [CL:unassigned ATP-binding cassette proteins:ATP-bindingcassette homology] [OR:Helicobacter pylori] [SR:strain J99, , strainJ99] [SR:strain J99, ] 238 SPX0475 475 3136 70 210 95 4.40E-07[LN:E72756] [AC:E72756] [PN:hypothetical protein APE0042] [GN:APE0042][OR:Aeropyrum pernix] 92 SPX0476 476 3137 122 366 256 3.70E-30[GI:5822822] [LN:AB024564] [AC:AB024564] [PN:YHCF] [GN:yhcF][OR:Bacillus halodurans] [SR:Bacillus halodurans (strain:C-125) DNA] 129SPX0477 477 3138 158 474 405 8.00E-51 [LN:E72221] [AC:E72221][PN:conserved hypothetical protein] [GN:TM1707] [CL:conservedhypothetical protein HI0943] [OR:Thermotoga maritima] 139 SPX0478 4783139 390 1170 NO-HIT 6 SPX0479 479 3140 299 897 300 2.40E-58[LN:DNAI_BACSU] [AC:P06567] [GN:DNAI] [OR:Bacillus subtilis][DE:PRIMOSOMAL PROTEIN DNAI] [SP:P06567] 101 SPX0480 480 3141 238 714239 3.90E-35 [LN:CHRR_PSESP] [AC:P96977] [GN:CHRR] [OR:Pseudomonas sp][SR:,strain G-1] [DE:CR(VI) REDUCTASE] [SP:P96977] 110 SPX0481 481 3142437 1311 1986 1.10E-270 [GI:6681650] [LN:AB016077] [AC:AB016077][PN:phosphoglycerate dehydrogenase] [GN:pgdA] [OR:Streptococcus mutans][SR:Streptococcus mutans (strain:MT8148) DNA, clone:pYT570] 174 SPX0482482 3143 115 345 NO-HIT 6 SPX0483 483 3144 118 354 NO-HIT 6 SPX0484 4843145 64 192 NO-HIT 6 SPX0485 485 3146 284 852 103 3.00E-11 [GI:4102023][LN:AF007761] [AC:AF007761] [PN:MutR] [GN:mutR] [FN:positivetranscriptional regulator of mutA] [OR:Streptococcus mutans] 134 SPX0486486 3147 131 393 NO-HIT 6 SPX0487 487 3148 264 792 NO-HIT 6 SPX0488 4883149 226 678 NO-HIT 6 SPX0489 489 3150 211 633 282 3.20E-42[LN:YYBJ_BACSU] [AC:P37494] [GN:YYBJ] [OR:Bacillus subtilis][DE:INTERGENIC REGION] [SP:P37494] 95 SPX0490 490 3151 96 288 NO-HIT 6SPX0491 491 3152 838 2514 989 0 [LN:SECA_LISMO] [AC:P47847] [GN:SECA][OR:Listeria monocytogenes] [DE:PREPROTEIN TRANSLOCASE SECA SUBUNIT][SP:P47847] 118 SPX0492 492 3153 344 1032 156 7.30E-47 [GI:7380801][LN:NMA7Z2491] [AC:AL162758:AL157959][PN:phospho-2-dehydr-3-deoxyheptonate aldolase] [GN:aroG] [OR:Neisseriameningitidis] 136 SPX0493 493 3154 215 645 178 3.50E-34 [LN:AROF_ECOLI][AC:P00888] [GN:AROF] [OR:Escherichia coli] [EC:4.1.2.15][DE:SYNTHETASE) (3-DEOXY-D-ARABINO-HEPTULOSONATE 7-PHOSPHATE SYNTHASE)][SP:P00888] 157 SPX0494 494 3155 111 333 NO-HIT 6 SPX0495 495 3156 89267 132 2.60E-14 [GI:7380801] [LN:NMA7Z2491] [AC:AL162758:AL157959][PN:phospho-2-dehydr-3-deoxyheptonate aldolase] [GN:aroG] [OR:Neisseriameningitidis] 136 SPX0496 496 3157 121 363 177 1.70E-30 [LN:H69772][AC:H69772] [PN:holo-[acyl-carrier-protein]synthase,] [GN:ydcB][CL:holo-ACP synthase] [OR:Bacillus subtilis] [EC:2.7.8.7] 137 SPX0497497 3158 368 1104 1852 1.10E-252 [GI:5759209] [LN:AF171873][AC:AF171873] [PN:alanine racemase] [GN:alr] [OR:Streptococcuspneumoniae] 101 SPX0498 498 3159 672 2016 3357 0 [LN:RECG_STRPN][AC:Q54900] [GN:RECG:MMSA] [OR:Streptococcus pneumoniae] [EC:3.6.1.-][DE:ATP-DEPENDENT DNA HELICASE RECG,] [SP:Q54900] 137 SPX0499 499 316089 267 263 2.70E-32 [LN:T30285] [AC:T30285] [PN:hypothetical protein][OR:Streptococcus pneumoniae] 79 SPX0500 500 3161 68 204 NO-HIT 6SPX0501 501 3162 327 981 447 1.40E-92 [GI:2353697] [LN:AF001926][AC:AF001926] [PN:xylan esterase 1] [GN:axe1] [OR:Thermoanaerobacteriumsp. ′JW/SL YS485′] 117 SPX0502 502 3163 206 618 355 1.20E-44 [LN:T30285][AC:T30285] [PN:hypothetical protein] [OR:Streptococcus pneumoniae] 79SPX0503 503 3164 168 504 172 1.10E-15 [GI:4101572] [LN:AF004842][AC:AF004842] [PN:major royal jelly protein MRJP5] [GN:MRJP5] [OR:Apismellifera] [SR:honeybee] 122 SPX0504 504 3165 76 228 371 3.40E-50[LN:T30286] [AC:T30286:S26297] [PN:hypothetical protein 76][OR:Streptococcus pneumoniae] 89 SPX0505 505 3166 938 2814 4378 0[LN:NANA_STRPN] [AC:Q59959:Q54722] [GN:NANA] [OR:Streptococcuspneumoniae] [EC:3.2.1.18] [DE:SIALIDASE A PRECURSOR, (NEURAMINIDASE A)][SP:Q59959:Q54722] 155 SPX0506 506 3167 72 216 NO-HIT 6 SPX0507 507 3168151 453 773 6.10E-103 [GI:1163111] [LN:SPU43526] [AC:U43526][OR:Streptococcus pneumoniae] 68 SPX0508 508 3169 446 1338 2307 0[GI:1163112] [LN:SPU43526] [AC:U43526] [OR:Streptococcus pneumoniae] 68SPX0509 509 3170 295 885 1542 2.00E-218 [GI:1163113] [LN:SPU43526][AC:U43526] [OR:Streptococcus pneumoniae] 68 SPX0510 510 3171 278 8341375 3.80E-192 [GI:1163114] [LN:SPU43526] [AC:U43526] [OR:Streptococcuspneumoniae] 68 SPX0511 511 3172 254 762 1250 1.40E-167 [LN:NANB_STRPN][AC:Q54727] [GN:NANB] [OR:Streptococcus pneumoniae] [EC:3.2.1.18][DE:SIALIDASE B PRECURSOR, (NEURAMINIDASE B)] [SP:Q54727] 141 SPX0512512 3173 126 378 333 1.60E-40 [GI:517210] [LN:SPU11799] [AC:U11799][OR:Streptococcus pyogenes] 65 SPX0513 513 3174 211 633 762 7.90E-101[GI:517210] [LN:SPU11799] [AC:U11799] [OR:Streptococcus pyogenes] 65SPX0514 514 3175 467 1401 2363 0 [LN:NANB_STRPN] [AC:Q54727] [GN:NANB][OR:Streptococcus pneumoniae] [EC:3.2.1.18] [DE:SIALIDASE B PRECURSOR,(NEURAMINIDASE B)] [SP:Q54727] 141 SPX0515 515 3176 368 1104 18381.30E-249 [LN:YJHC_STRPN] [AC:Q54728] [OR:Streptococcus pneumoniae][DE:HYPOTHETICAL PROTEIN IN NANB 3′REGION (ORF-5) (FRAGMENT)][SP:Q54728] 131 SPX0516 516 3177 130 390 NO-HIT 6 SPX0517 517 3178 233699 331 1.90E-64 [LN:C70180] [AC:C70180] [PN:conserved hypotheticalprotein BB0644] [OR:Borrelia burgdorferi] [SR:, Lyme disease spirochete]125 SPX0518 518 3179 506 1518 839 2.60E-178 [LN:D70180] [AC:D70180][PN:phosphotransferase system enzyme II,, glucose-specific, factor II][OR:Borrelia burgdorferi] [SR:, Lyme disease spirochete] [EC:2.7.1.69]167 SPX0519 519 3180 443 1329 110 1.90E-09 [GI:6137033] [LN:SCF11][AC:AL132662] [PN:putative sugar transporter sugar binding][GN:SCF11.11] [OR:Streptomyces coelicolor A3(2)] 132 SPX0520 520 3181296 888 211 1.60E-50 [LN:E72357] [AC:E72357] [PN:sugar ABC transporter,permease protein] [GN:TM0596] [CL:inner membrane protein malF][OR:Thermotoga maritima] 140 SPX0521 521 3182 280 840 434 1.10E-65[LN:F72379] [AC:F72379] [PN:sugar ABC transporter, permease protein][GN:TM0430] [CL:maltose transport protein malG] [OR:Thermotoga maritima]143 SPX0522 522 3183 151 453 109 2.60E-13 [LN:YJGK_ECOLI] [AC:P39335][GN:YJGK] [OR:Escherichia coli] [DE:HYPOTHETICAL 17.3 KD PROTEIN INPYRL-ARGI INTERGENIC REGION (O153B)] [SP:P39335] 144 SPX0523 523 3184118 354 NO-HIT 6 SPX0524 524 3185 66 198 NO-HIT 6 SPX0525 525 3186 215645 NO-HIT 6 SPX0526 526 3187 220 660 830 1.30E-109 [GI:2385360][LN:CTSIALIDA] [AC:Y08695] [PN:putative acylneuraminate lyase][OR:Clostridium tertium] 100 SPX0527 527 3188 100 300 68 0.00016[GI:42131] [LN:ECNPL] [AC:X03345] [OR:Escherichia coli] 55 SPX0528 5283189 295 885 423 2.50E-53 [LN:YNGA_CLOPE] [AC:P26832] [OR:Clostridiumperfringens] [DE:HYPOTHETICAL PROTEIN IN NAGH 5′REGION (ORFA)(FRAGMENT)] [SP:P26832] 129 SPX0529 529 3190 283 849 170 2.10E-25[LN:Y143_HAEIN] [AC:P44540] [GN:HI0143] [OR:Haemophilus influenzae][DE:HYPOTHETICAL PROTEIN HI0143] [SP:P44540] 112 SPX0530 530 3191 6812043 3365 0 [GI:4009463] [LN:AF068901] [AC:AF068901][PN:penicillin-binding protein 2b] [GN:pbp2b] [OR:Streptococcuspneumoniae] 116 SPX0531 531 3192 119 357 524 5.00E-69 [GI:49383][LN:SPPBP2BH] [AC:Z21808] [PN:internal region of the penicillin-binding][FN:penicillin-resistantance] [OR:Streptococcus pneumoniae] 143 SPX0532532 3193 171 513 625 4.80E-83 [GI:4009464] [LN:AF068901] [AC:AF068901][PN:RecM] [GN:recM] [OR:Streptococcus pneumoniae] 90 SPX0533 533 3194348 1044 1766 1.30E-239 [GI:4009465] [LN:AF068901] [AC:AF068901][PN:D-Ala-D-Ala ligase] [GN:ddl] [OR:Streptococcus pneumoniae] 103SPX0534 534 3195 458 1374 2278 0 [GI:4009466] [LN:AF068901][AC:AF068901] [PN:D-Ala-D-Ala adding enzyme] [GN:murF] [OR:Streptococcuspneumoniae] 111 SPX0535 535 3196 449 1347 403 3.50E-76 [GI:5822769][LN:AB024553] [AC:AB024553] [OR:Bacillus halodurans] [SR:Bacillushalodurans (strain:C-125) DNA] 109 SPX0536 536 3197 192 576 9541.80E-127 [GI:4009467] [LN:AF068901] [AC:AF068901] [PN:MutT] [GN:mutT][OR:Streptococcus pneumoniae] 90 SPX0537 537 3198 199 597 1003 1.80E-140[GI:4009468] [LN:AF068901] [AC:AF068901] [PN:unknown] [OR:Streptococcuspneumoniae] 83 SPX0538 538 3199 87 261 NO-HIT 6 SPX0539 539 3200 4581374 2266 0 [GI:4009469] [LN:AF068901] [AC:AF068901] [PN:cell divisionprotein FtsA] [GN:ftsA] [OR:Streptococcus pneumoniae] 112 SPX0540 5403201 419 1257 2094 4.10E-280 [GI:4009470] [LN:AF068901] [AC:AF068901][PN:cell division protein FtsZ] [GN:ftsZ] [OR:Streptococcus pneumoniae]112 SPX0541 541 3202 79 237 178 2.40E-19 [LN:A71218] [AC:A71218][PN:hypothetical protein PH0004] [GN:PH0004] [OR:Pyrococcus horikoshii]95 SPX0542 542 3203 224 672 1101 6.20E-148 [GI:4009471] [LN:AF068901][AC:AF068901] [PN:YlmE] [GN:ylmE] [OR:Streptococcus pneumoniae] 90SPX0543 543 3204 180 540 920 1.10E-122 [GI:4009472] [LN:AF068901][AC:AF068901] [PN:YlmF] [GN:ylmF] [OR:Streptococcus pneumoniae] 90SPX0544 544 3205 88 264 431 1.50E-58 [GI:4009473] [LN:AF068901][AC:AF068901] [PN:YlmG] [GN:ylmG] [OR:Streptococcus pneumoniae] 90SPX0545 545 3206 262 786 1318 2.10E-179 [GI:4009474] [LN:AF068901][AC:AF068901] [PN:YlmH] [GN:ylmH] [OR:Streptococcus pneumoniae] 90SPX0546 546 3207 263 789 1297 1.90E-171 [GI:4009475] [LN:AF068901][AC:AF068901] [PN:cell division protein DivIVA] [GN:divIVA][OR:Streptococcus pneumoniae] 116 SPX0547 547 3208 931 2793 4840 0[GI:4009476] [LN:AF068901] [AC:AF068901] [PN:isoleucine-tRNA synthetase][GN:ileS] [OR:Streptococcus pneumoniae] 112 SPX0548 548 3209 62 186 820.00016 [LN:A56034] [AC:A56034] [PN:insulin activator factor] [CL:humaninsulin activator factor] [OR:Homo sapiens] [SR:, man] 120 SPX0549 5493210 87 261 192 2.20E-20 [LN:A56034] [AC:A56034] [PN:insulin activatorfactor] [CL:human insulin activator factor] [OR:Homo sapiens] [SR:, man]120 SPX0550 550 3211 63 189 NO-HIT 6 SPX0551 551 3212 72 216 NO-HIT 6SPX0552 552 3213 231 693 1201 1.00E-160 [GI:5578891] [LN:SPN131985][AC:AJ131985] [PN:phosphoglyceromutase] [GN:gpmA] [OR:Streptococcuspneumoniae] 107 SPX0553 553 3214 804 2412 232 2.70E-95 [GI:5912520][LN:SCF12] [AC:AL117669] [PN:putative large secreted protein][GN:SCF12.20c] [OR:Streptomyces coelicolor A3(2)] 124 SPX0554 554 3215237 711 642 7.20E-84 [LN:B69477] [AC:B69477] [PN:ABC transporter,ATP-binding protein homolog] [CL:unassigned ATP-binding cassetteproteins:ATP-binding cassette homology] [OR:Archaeoglobus fulgidus] 179SPX0555 555 3216 925 2775 106 1.10E-16 [LN:C69477] [AC:C69477][PN:hypothetical protein AF1820] [OR:Archaeoglobus fulgidus] 84 SPX0556556 3217 173 519 878 1.10E-117 [GI:4193357] [LN:AF055088][AC:AF055088:AF055087] [PN:putative hydrophobic transmembrane protein][GN:psaD] [OR:Streptococcus pneumoniae] 137 SPX0557 557 3218 310 9301579 2.30E-209 [GI:3258602] [LN:SPU40786] [AC:U40786] [PN:surfaceantigen A variant precursor] [GN:psaA] [FN:putative fimbrial adhesin][OR:Streptococcus pneumoniae] 150 SPX0558 558 3219 283 849 11718.00E-165 [LN:P29K_STRGC] [AC:P42361] [OR:Streptococcus gordoniichallis] [DE:29 KD MEMBRANE PROTEIN IN PSAA 5′REGION (ORF1)] [SP:P42361]127 SPX0559 559 3220 252 756 1208 2.80E-164 [GI:4193356] [LN:AF055088][AC:AF055088:AF055087] [PN:ATP-binding cassette] [GN:psaB][OR:Streptococcus pneumoniae] 115 SPX0560 560 3221 651 1953 1477 0[GI:5139244] [LN:AF116532] [AC:AF116532] [PN:endopeptidase O] [GN:pepO][OR:Streptococcus parasanguinis] 104 SPX0561 561 3222 210 630 1812.90E-36 [LN:YQGX_BACSU] [AC:P54501] [GN:YQGX] [OR:Bacillus subtilis][DE:HYPOTHETICAL 23.2 KD PROTEIN IN SODA-COMGA INTERGENIC REGION][SP:P54501] 138 SPX0562 562 3223 67 201 131 2.00E-13 [GI:1914870][LN:SPZ82001] [AC:Z82001] [PN:unknown] [OR:Streptococcus pneumoniae] 81SPX0563 563 3224 81 243 NO-HIT 6 SPX0564 564 3225 741 2223 1601 0[LN:RELA_STREQ] [AC:Q54089] [GN:RELA:REL] [OR:Streptococcus equisimilis][EC:2.7.6.5] [DE:PROTEIN)] [SP:Q54089] 111 SPX0565 565 3226 81 243 700.0001 [LN:Q3ECS7] [AC:A30374:Q90796] [PN:hypothetical 77K protein (spoT3′region)] [CL:Escherichia coli hypothetical 77K protein (spoT3′region)] [OR:Escherichia coli] 163 SPX0566 566 3227 148 444 5852.40E-76 [LN:S39974] [AC:S39974] [PN:hypothetical protein] [CL:conservedhypothetical protein HI0670] [OR:Streptococcus equisimilis] 123 SPX0567567 3228 76 228 NO-HIT 6 SPX0568 568 3229 141 423 NO-HIT 6 SPX0569 5693230 236 708 NO-HIT 6 SPX0570 570 3231 140 420 433 7.90E-56 [GI:6694218][LN:AF182402] [AC:AF182402] [PN:metalloregulator RmtA] [GN:rmtA][OR:Streptococcus gordonii] 105 SPX0571 571 3232 80 240 307 4.00E-38[GI:6694218] [LN:AF182402] [AC:AF182402] [PN:metalloregulator RmtA][GN:rmtA] [OR:Streptococcus gordonii] 105 SPX0572 572 3233 281 843 1252.00E-13 [LN:G75297] [AC:G75297] [PN:conserved hypothetical protein][GN:DR2233] [CL:probable phosphoesterase MJ0912:phosphoesterase corehomology] [OR:Deinococcus radiodurans] 167 SPX0573 573 3234 65 195NO-HIT 6 SPX0574 574 3235 105 315 142 7.90E-15 [LN:D70063] [AC:D70063][PN:hypothetical protein ywnA] [GN:ywnA] [OR:Bacillus subtilis] 87SPX0575 575 3236 73 219 129 2.40E-12 [LN:D70063] [AC:D70063][PN:hypothetical protein ywnA] [GN:ywnA] [OR:Bacillus subtilis] 87SPX0576 576 3237 101 303 NO-HIT 6 SPX0577 577 3238 358 1074 NO-HIT 6SPX0578 578 3239 226 678 1146 1.70E-157 [GI:5830520] [LN:SPAJ6391][AC:AJ006391] [PN:response regulator] [GN:rr01] [OR:Streptococcuspneumoniae] 104 SPX0579 579 3240 325 975 1628 3.20E-226 [GI:5830521][LN:SPAJ6391] [AC:AJ006391] [PN:histidine kinase] [GN:hk01][OR:Streptococcus pneumoniae] 102 SPX0580 580 3241 661 1983 11492.20E-274 [LN:SYT1_BACSU] [AC:P18255:P06570] [GN:THRS:THRSV][OR:Bacillus subtilis] [EC:6.1.1.3] [DE:(THRRS)] [SP:P18255:P06570] 118SPX0581 581 3242 130 390 NO-HIT 6 SPX0582 582 3243 97 291 NO-HIT 6SPX0583 583 3244 70 210 NO-HIT 6 SPX0584 584 3245 210 630 371 1.30E-60[LN:E70063] [AC:E70063] [PN:hypothetical protein ywnB] [GN:ywnB][OR:Bacillus subtilis] 87 SPX0585 585 3246 90 270 311 1.10E-38[LN:F69700] [AC:F69700:S11365:S70690] [PN:ribosomal protein S15(rpsO):ribosomal protein BS18] [GN:rpsO] [CL:Escherichia coli ribosomalprotein S15:eubacterial ribosomal protein S15 homology] [OR:Bacillussubtilis] 214 SPX0586 586 3247 75 225 NO-HIT 6 SPX0587 587 3248 159 477243 1.30E-38 [GI:1916729] [LN:AF134905] [AC:AF134905:U76550] [PN:CadD][GN:cadD] [OR:Staphylococcus aureus] 94 SPX0588 588 3249 250 750 1651.10E-23 [LN:E69826] [AC:E69826] [PN:1-acylglycerol-3-phosphateO-acyltransfera homolog yhdO] [GN:yhdO] [OR:Bacillus subtilis] 117SPX0589 589 3250 779 2337 414 1.80E-126 [LN:CTPE_MYCTU] [AC:O08365][GN:CTPE:RV0908:MTCY21C12.02] [OR:Mycobacterium tuberculosis][EC:3.6.1.-] [DE:PROBABLE CATION-TRANSPORTING ATPASE E,] [SP:O08365] 160SPX0590 590 3251 77 231 NO-HIT 6 SPX0591 591 3252 488 1464 122 9.60E-23[GI:1480429] [LN:BSU18943] [AC:U18943:X99465] [GN:MtlR] [OR:Bacillusstearothermophilus] 88 SPX0592 592 3253 143 429 60 0.00018 [GI:2317740][LN:AF013987] [AC:AF013987] [PN:nitrogen regulatory IIA protein][GN:ptsN] [OR:Vibrio cholerae] 108 SPX0593 593 3254 151 453 223 5.60E-24[LN:HRSA_ECOLI] [AC:P54745] [GN:HRSA] [OR:Escherichia coli][EC:2.7.1.69] [DE:HRSA PROTEIN,] [SP:P54745] 106 SPX0594 594 3255 104312 236 1.30E-27 [LN:PTWB_ECOLI] [AC:P32673] [GN:FRWB] [OR:Escherichiacoli] [EC:2.7.1.69] [DE:II, B COMPONENT),] [SP:P32673] 110 SPX0595 5953256 369 1107 398 8.00E-60 [LN:PTFB_XANCP] [AC:P23355] [GN:FRUA][OR:Xanthomonas campestris] [SR:,pvcampestris] [EC:2.7.1.69] [DE:(EC2.7.1.69) (EII-FRU)] [SP:P23355] 141 SPX0596 596 3257 232 696 5606.50E-74 [LN:ALSE_ECOLI] [AC:P32719] [GN:ALSE] [OR:Escherichia coli][EC:5.1.3.-] [DE:D-ALLULOSE-6-PHOSPHATE 3-EPIMERASE,] [SP:P32719] 127SPX0597 597 3258 657 1971 1371 2.00E-292 [LN:TKT_STRPN] [AC:P22976][GN:RECP] [OR:Streptococcus pneumoniae] [EC:2.2.1.1] [DE:PROBABLETRANSKETOLASE, (TK)] [SP:P22976] 127 SPX0598 598 3259 191 573 4222.30E-53 [LN:B30868] [AC:B30868] [PN:hypothetical protein 1][OR:Streptococcus agalactiae] 81 SPX0599 599 3260 191 573 422 2.30E-53[LN:B30868] [AC:B30868] [PN:hypothetical protein 1] [OR:Streptococcusagalactiae] 81 SPX0600 600 3261 278 834 587 1.60E-140 [LN:A33595][AC:A33595:A30868] [PN:probable transposase] [CL:transposase IS3][OR:Streptococcus agalactiae] 107 SPX0601 601 3262 177 531 NO-HIT 6SPX0602 602 3263 139 417 138 1.40E-10 [LN:T35180] [AC:T35180][PN:hypothetical protein SC5A7.31] [GN:SC5A7.31] [CL:Streptomycescoelicolor hypothetical protein SC5A7.31] [OR:Streptomyces coelicolor]160 SPX0603 603 3264 226 678 612 1.10E-79 [GI:1813343] [LN:D78182][AC:D78182] [GN:ORF3] [OR:Streptococcus mutans] [SR:Streptococcus mutans(strain:Xc) DNA] 114 SPX0604 604 3265 266 798 344 5.40E-120 [GI:1813344][LN:D78182] [AC:D78182] [GN:ORF4] [OR:Streptococcus mutans][SR:Streptococcus mutans (strain:Xc) DNA] 114 SPX0605 605 3266 368 1104335 4.50E-71 [LN:YURR_BACSU] [AC:O32159] [GN:YURR] [OR:Bacillussubtilis] [DE:HYPOTHETICAL 39.4 KD OXIDOREDUCTASE IN HOM-MRGA INTERGENICREGION] [SP:O32159] 143 SPX0606 606 3267 64 192 NO-HIT 6 SPX0607 6073268 340 1020 1167 7.10E-156 [LN:GALE_BACSU] [AC:P55180] [GN:GALE][OR:Bacillus subtilis] [EC:5.1.3.2] [DE:GALACTOSE 4-EPIMERASE)][SP:P55180] 113 SPX0608 608 3269 318 954 441 7.80E-87 [LN:CSBB_BACSU][AC:Q45539] [GN:CSBB] [OR:Bacillus subtilis] [DE:CSBB PROTEIN][SP:Q45539] 90 SPX0609 609 3270 222 666 NO-HIT 6 SPX0610 610 3271 69 20755 0.00029 [LN:FER_MOOTH] [AC:P00203] [OR:Moorella thermoacetica][SR:,Clostridium thermoaceticum] [DE:FERREDOXIN] [SP:P00203] 117 SPX0611611 3272 159 477 NO-HIT 6 SPX0612 612 3273 224 672 413 6.00E-74[LN:KCY_BACSU] [AC:P38493] [GN:CMK:JOFC] [OR:Bacillus subtilis][EC:2.7.4.14] [DE:(CMP KINASE)] [SP:P38493] 107 SPX0613 613 3274 113 339432 5.60E-55 [LN:PHNA_ECOLI] [AC:P16680] [GN:PHNA] [OR:Escherichia coli][DE:PHNA PROTEIN] [SP:P16680] 89 SPX0614 614 3275 210 630 NO-HIT 6SPX0615 615 3276 76 228 192 3.60E-23 [GI:1914870] [LN:SPZ82001][AC:Z82001] [PN:unknown] [OR:Streptococcus pneumoniae] 81 SPX0616 6163277 384 1152 68 6.80E-05 [LN:C81266] [AC:C81266] [PN:probable effluxprotein Cj1687 [imported]] [GN:Cj1687] [OR:Campylobacter jejuni] 108SPX0617 617 3278 250 750 309 4.30E-69 [LN:TRUA_BACSU] [AC:P70973][GN:TRUA] [OR:Bacillus subtilis] [EC:4.2.1.70] [DE:I) (PSEUDOURIDINESYNTHASE I) (URACIL HYDROLYASE)] [SP:P70973] 141 SPX0618 618 3279 258774 155 3.70E-39 [LN:THID_BACSU] [AC:P39610] [GN:THID:IPA-52R][OR:Bacillus subtilis] [EC:2.7.4.7] [DE:(HMP-P KINASE)] [SP:P39610] 113SPX0619 619 3280 154 462 69 5.80E-12 [LN:G75153] [AC:G75153][PN:hypothetical protein PAB2090] [GN:PAB2090] [OR:Pyrococcus abyssi] 93SPX0620 620 3281 191 573 422 2.30E-53 [LN:B30868] [AC:B30868][PN:hypothetical protein 1] [OR:Streptococcus agalactiae] 81 SPX0621 6213282 91 273 288 2.30E-35 [LN:A33595] [AC:A33595:A30868] [PN:probabletransposase] [CL:transposase IS3] [OR:Streptococcus agalactiae] 107SPX0622 622 3283 198 594 583 9.30E-95 [LN:A33595] [AC:A33595:A30868][PN:probable transposase] [CL:transposase IS3] [OR:Streptococcusagalactiae] 107 SPX0623 623 3284 159 477 NO-HIT 6 SPX0624 624 3285 3611083 1016 1.20E-136 [GI:2323341] [LN:AF014460] [AC:AF014460] [PN:PepQ][FN:hydrolysis of Leu-Pro] [OR:Streptococcus mutans] 103 SPX0625 6253286 261 783 147 5.10E-36 [LN:T31439] [AC:T31439] [PN:probable cobyricacid synthase CobQ] [OR:Heliobacillus mobilis] 91 SPX0626 626 3287 4481344 137 1.30E-46 [LN:T31440] [AC:T31440] [PN:UDP-N-acetylmuramyltripeptide synthetase homolog murC] [OR:Heliobacillus mobilis] 110SPX0627 627 3288 439 1317 797 4.80E-136 [LN:YKGC_ECOLI] [AC:P77212][GN:YKGC] [OR:Escherichia coli] [DE:INTERGENIC REGION] [SP:P77212] 94SPX0628 628 3289 291 873 711 3.70E-137 [GI:7107009] [LN:AF168363][AC:AF168363] [PN:oxalate:formate antiporter] [OR:Lactococcus lactis] 96SPX0629 629 3290 82 246 193 5.00E-21 [GI:7107009] [LN:AF168363][AC:AF168363] [PN:oxalate:formate antiporter] [OR:Lactococcus lactis] 96SPX0630 630 3291 525 1575 1329 1.80E-184 [GI:4409804] [LN:AF091502][AC:AF091502] [PN:autoaggregation-mediating protein] [GN:aggH][OR:Lactobacillus reuteri] 116 SPX0631 631 3292 263 789 547 3.10E-74[LN:CODY_BACSU] [AC:P39779] [GN:CODY] [OR:Bacillus subtilis] [DE:CODYPROTEIN (VEGETATIVE PROTEIN 286B) (VEG286B)] [SP:P39779] 126 SPX0632 6323293 69 207 174 1.30E-18 [LN:C70008] [AC:C70008][PN:pyrazinamidase/nicotinamidase homolog yueJ] [GN:yueJ][CL:hypothetical protein b1011] [OR:Bacillus subtilis] 136 SPX0633 6333294 152 456 253 1.50E-30 [LN:C70008] [AC:C70008][PN:pyrazinamidase/nicotinamidase homolog yueJ] [GN:yueJ][CL:hypothetical protein b1011] [OR:Bacillus subtilis] 136 SPX0634 6343295 78 234 328 1.70E-40 [GI:600072] [LN:SEDEXB] [AC:X72832] [PN:ABCtransporter] [GN:abc] [OR:Streptococcus equisimilis] 96 SPX0635 635 329652 156 113 2.50E-10 [LN:E72756] [AC:E72756] [PN:hypothetical proteinAPE0042] [GN:APE0042] [OR:Aeropyrum pernix] 92 SPX0636 636 3297 285 855731 1.70E-136 [LN:MSMK_STRMU] [AC:Q00752] [GN:MSMK] [OR:Streptococcusmutans] [DE:MULTIPLE SUGAR-BINDING TRANSPORT ATP-BINDING PROTEIN MSMK][SP:Q00752] 138 SPX0637 637 3298 253 759 485 3.90E-95 [LN:Y095_HAEIN][AC:Q57060:O05007] [GN:HI0095] [OR:Haemophilus influenzae][DE:HYPOTHETICAL PROTEIN HI0095] [SP:Q57060:O05007] 126 SPX0638 638 3299177 531 603 2.90E-79 [LN:B69587] [AC:B69587] [PN:adeninephosphoribosyltransferase,:AMP pyrophosphorylase:transphosphoribosidase][GN:apt] [CL:adenine phosphoribosyltransferase] [OR:Bacillus subtilis][EC:2.4.2.7] 194 SPX0639 639 3300 315 945 567 6.90E-116 [LN:C72324][AC:C72324] [PN:homoserine O-succinyltransferase] [GN:TM0881][CL:homoserine succinyltransferase] [OR:Thermotoga maritima] 134 SPX0640640 3301 226 678 357 5.50E-90 [GI:1813342] [LN:D78182] [AC:D78182][GN:ORF2] [OR:Streptococcus mutans] [SR:Streptococcus mutans (strain:Xc)DNA] 114 SPX0641 641 3302 125 375 NO-HIT 6 SPX0642 642 3303 253 759 8641.30E-113 [LN:TPIS_LACDE] [AC:O32757] [GN:TPIA:TPI] [OR:Lactobacillusdelbrueckii] [SR:,subspbulgaricus] [EC:5.3.1.1] [DE:TRIOSEPHOSPHATEISOMERASE, (TIM)] [SP:O32757] 159 SPX0643 643 3304 502 1506 2728 0[GI:4218526] [LN:SPAJ9639] [AC:AJ009639][PN:1,4-beta-N-acetylmuramidase] [GN:lytC] [FN:lysis of cell wallpeptidoglycan] [OR:Streptococcus pneumoniae] 153 SPX0644 644 3305 173519 800 2.60E-105 [GI:3513547] [LN:AF055720] [AC:AF055720] [PN:unknown][OR:Streptococcus pneumoniae] 83 SPX0645 645 3306 213 639 NO-HIT 6SPX0646 646 3307 169 507 882 2.00E-118 [GI:2196662] [LN:HSZ84379][AC:Z84379] [PN:dihydrofolate reductase] [GN:dfr] [FN:trimethoprimresistance] [OR:Streptococcus pneumoniae] 135 SPX0647 647 3308 69 207NO-HIT 6 SPX0648 648 3309 411 1233 1251 4.80E-206 [GI:7546983][LN:AF236863] [AC:AF236863] [PN:protease ClpX] [GN:clpX] [OR:Lactococcuslactis] 93 SPX0649 649 3310 196 588 807 9.70E-107 [GI:7546984][LN:AF236863] [AC:AF236863] [PN:hypothetical GTP-binding protein][OR:Lactococcus lactis] 102 SPX0650 650 3311 127 381 392 2.30E-49[LN:ALDR_LACLA] [AC:O34133] [GN:ALDR] [OR:Lactococcus lactis][SR:,subsplactis:Streptococcus lactis] [DE:PUTATIVE REGULATOR ALDR][SP:O34133] 143 SPX0651 651 3312 297 891 337 2.00E-91 [GI:7328270][LN:SAY14324] [AC:Y14324] [PN:hypothetical protein] [OR:Staphylococcusaureus] 91 SPX0652 652 3313 326 978 268 1.30E-62 [LN:YVCK_BACSU][AC:O06974] [GN:YVCK] [OR:Bacillus subtilis] [DE:HYPOTHETICAL 34.7 KDPROTEIN IN CRH-TRXB INTERGENIC REGION] [SP:O06974] 136 SPX0653 653 3314304 912 424 5.50E-81 [GI:7328272] [LN:SAY14324] [AC:Y14324][OR:Staphylococcus aureus] 65 SPX0654 654 3315 323 969 422 5.00E-99[LN:B70015] [AC:B70015] [PN:thioredoxin reductase homolog yumC][GN:yumC] [CL:thioredoxin reductase:thioredoxin reductase homology][OR:Bacillus subtilis] 154 SPX0655 655 3316 272 816 419 8.50E-81[LN:H69744] [AC:H69744] [PN:conserved hypothetical protein ybbP][GN:ybbP] [CL:hypothetical protein ybbP] [OR:Bacillus subtilis] 128SPX0656 656 3317 260 780 104 2.70E-10 [LN:A69745] [AC:A69745][PN:hypothetical protein ybbR] [GN:ybbR] [OR:Bacillus subtilis] 87SPX0657 657 3318 64 192 NO-HIT 6 SPX0658 658 3319 451 1353 655 2.00E-180[GI:3892895] [LN:SAARGFEMD] [AC:Y15477] [PN:phosphoglucosamine-mutase][GN:glmM] [OR:Staphylococcus aureus] 107 SPX0659 659 3320 121 363 NO-HIT6 SPX0660 660 3321 283 849 239 6.50E-25 [LN:DEGV_BACSU] [AC:P32436][GN:DEGV] [OR:Bacillus subtilis] [DE:DEGV PROTEIN] [SP:P32436] 90SPX0661 661 3322 256 768 614 6.50E-89 [LN:DAPB_BACSU] [AC:P42976][GN:DAPB] [OR:Bacillus subtilis] [EC:1.3.1.26] [DE:DIHYDRODIPICOLINATEREDUCTASE,] [SP:P42976] 124 SPX0662 662 3323 400 1200 601 8.40E-92[LN:PAPS_BACSU] [AC:P42977] [GN:PAPS] [OR:Bacillus subtilis][EC:2.7.7.19] [DE:POLY(A) POLYMERASE, (PAP)] [SP:P42977] 119 SPX0663 6633324 624 1872 669 1.80E-162 [LN:A69814] [AC:A69814] [PN:ABC transporter(ATP-binding protein) homolog yfmR] [GN:yfmR] [CL:unassigned ATP-bindingcassette proteins:ATP-binding cassette homology] [OR:Bacillus subtilis]188 SPX0664 664 3325 144 432 NO-HIT 6 SPX0665 665 3326 394 1182 6291.90E-82 [LN:YEAB_BACSU] [AC:P46348:O05001] [GN:YEAB] [OR:Bacillussubtilis] [DE:HYPOTHETICAL 31.8 KD PROTEIN IN GABP-GUAA INTERGENICREGION (ORFX)] [SP:P46348:O05001] 158 SPX0666 666 3327 899 2697 6011.20E-189 [LN:S77052] [AC:S77052] [PN:cation-transporting ATPase,pacL-1:protein sll0672:protein sll0672] [GN:pacL-1][CL:Na+/K+-transporting ATPase alpha chain:ATPase nucleotide-bindingdomain homology] [OR:Synechocystis sp.] 218 SPX0667 667 3328 97 291NO-HIT 6 SPX0668 668 3329 83 249 73 0.00016 [LN:H72624] [AC:H72624][PN:hypothetical protein APE1456] [GN:APE1456] [OR:Aeropyrum pernix] 92SPX0669 669 3330 264 792 713 2.30E-105 [LN:YGHU_ECOLI] [AC:Q46845][GN:YGHU] [OR:Escherichia coli] [DE:HYPOTHETICAL 34.2 KD PROTEIN INGSP-HYBG INTERGENIC REGION] [SP:Q46845] 135 SPX0670 670 3331 152 456 3683.30E-46 [LN:DEF_CLOBE] [AC:O08450] [GN:DEF:FMS] [OR:Clostridiumbeijerinckii] [SR:,Clostridium MP] [EC:3.5.1.31] [DE:DEFORMYLASE)][SP:O08450] 136 SPX0671 671 3332 532 1596 NO-HIT 6 SPX0672 672 3333 60180 NO-HIT 6 SPX0673 673 3334 243 729 473 1.20E-60 [GI:4580623][LN:AF118389] [AC:AF118389] [PN:unknown] [OR:Streptococcus suis] 77SPX0674 674 3335 210 630 111 2.10E-12 [GI:6562870] [LN:SCM1][AC:AL133422] [PN:putative secreted protein.] [GN:SCM1.21][OR:Streptomyces coelicolor A3(2)] 116 SPX0675 675 3336 163 489 680.00021 [LN:YPMB_BACSU] [AC:P54396] [GN:YPMB] [OR:Bacillus subtilis][DE:HYPOTHETICAL 17.9 KD PROTEIN IN DING-ASPB INTERGENIC REGION][SP:P54396] 137 SPX0676 676 3337 396 1188 1400 2.80E-187 [GI:6465901][LN:AF035157] [AC:AF035157] [PN:aspartate aminotransferase] [GN:aspC][OR:Lactococcus lactis] 106 SPX0677 677 3338 124 372 178 1.90E-27[LN:T03486] [AC:T03486] [PN:conserved hypothetical protein][OR:Rhodobacter capsulatus] 87 SPX0678 678 3339 448 1344 703 1.60E-180[LN:SYN_BACSU] [AC:P39772] [GN:ASNS] [OR:Bacillus subtilis][EC:6.1.1.22] [DE:(ASNRS)] [SP:P39772] 98 SPX0679 679 3340 129 387NO-HIT 6 SPX0680 680 3341 97 291 236 7.30E-39 [LN:RS6_BACSU] [AC:P21468][GN:RPSF] [OR:Bacillus subtilis] [DE:30S RIBOSOMAL PROTEIN S6 (BS9)][SP:P21468] 107 SPX0681 681 3342 157 471 481 5.20E-71 [GI:6716352][LN:AF145054] [AC:AF145054:AF001793:AF118440:U89246] [PN:ORF9] [GN:orf9][OR:Streptococcus thermophilus bacteriophage 7201] 136 SPX0682 682 334387 261 134 1.30E-13 [LN:RS18_BACST] [AC:P10806] [GN:RPSR] [OR:Bacillusstearothermophilus] [DE:30S RIBOSOMAL PROTEIN S18 (BS21)] [SP:P10806]120 SPX0683 683 3344 112 336 NO-HIT 6 SPX0684 684 3345 467 1401 2707.50E-47 [GI:4678225] [LN:AC007135] [AC:AC007135:AE002093][PN:cyclophilin-like protein] [GN:At2g36130] [OR:Arabidopsis thaliana][SR:thale cress] 137 SPX0685 685 3346 84 252 172 6.10E-19[LN:YABR_BACSU] [AC:P37560] [GN:YABR] [OR:Bacillus subtilis][DE:HYPOTHETICAL 14.2 KD PROTEIN IN DIVIC-SPOIIE INTERGENIC REGION][SP:P37560] 140 SPX0686 686 3347 87 261 96 1.40E-15 [LN:YABB_BACSU][AC:P37543] [GN:YABB] [OR:Bacillus subtilis] [DE:HYPOTHETICAL 28.3 KDPROTEIN IN XPAC-ABRB INTERGENIC REGION] [SP:P37543] 137 SPX0687 687 334867 201 109 3.00E-09 [LN:YABB_BACSU] [AC:P37543] [GN:YABB] [OR:Bacillussubtilis] [DE:HYPOTHETICAL 28.3 KD PROTEIN IN XPAC-ABRB INTERGENICREGION] [SP:P37543] 137 SPX0688 688 3349 129 387 267 1.40E-39[LN:YABB_BACSU] [AC:P37543] [GN:YABB] [OR:Bacillus subtilis][DE:HYPOTHETICAL 28.3 KD PROTEIN IN XPAC-ABRB INTERGENIC REGION][SP:P37543] 137 SPX0689 689 3350 93 279 224 1.50E-26 [LN:A69742][AC:A69742] [PN:conserved hypothetical protein yazA] [GN:yazA][CL:hypothetical protein 312] [OR:Bacillus subtilis] 127 SPX0690 6903351 60 180 143 5.60E-14 [GI:1743856] [LN:SGU57759] [AC:U57759][PN:intrageneric coaggregation-relevant adhesin] [OR:Streptococcusgordonii] 115 SPX0691 691 3352 222 666 955 2.60E-126 [GI:1743856][LN:SGU57759] [AC:U57759] [PN:intrageneric coaggregation-relevantadhesin] [OR:Streptococcus gordonii] 115 SPX0692 692 3353 171 513 NO-HIT6 SPX0693 693 3354 105 315 140 1.80E-21 [GI:2952534] [LN:AF051356][AC:AF051356] [PN:unknown] [OR:Streptococcus mutans] 79 SPX0694 694 335595 285 NO-HIT 6 SPX0695 695 3356 65 195 74 0.00038 [GI:2772940][LN:AF034574] [AC:AF034574] [PN:putative cruciform DNA binding protein][GN:Gv1] [OR:Glomus versiforme] 116 SPX0696 696 3357 504 1512 1721.50E-35 [LN:MURE_BACSU] [AC:Q03523] [GN:MURE] [OR:Bacillus subtilis][EC:6.3.2.13] [DE:DIAMINOPIMELATE-ADDING ENZYME)] [SP:Q03523] 122SPX0697 697 3358 192 576 172 9.40E-16 [LN:MURE_BACSU] [AC:Q03523][GN:MURE] [OR:Bacillus subtilis] [EC:6.3.2.13][DE:DIAMINOPIMELATE-ADDING ENZYME)] [SP:Q03523] 122 SPX0698 698 3359 5411623 187 2.90E-75 [LN:G69992] [AC:G69992] [PN:spore cortex proteinhomolog ytgP] [GN:ytgP] [OR:Bacillus subtilis] 95 SPX0699 699 3360 6531959 3335 0 [LN:ALIB_STRPN] [AC:Q51933] [GN:ALIB] [OR:Streptococcuspneumoniae] [DE:OLIGOPEPTIDE-BINDING PROTEIN ALIB PRECURSOR] [SP:Q51933]128 SPX0700 700 3361 185 555 282 2.00E-38 [GI:1125685] [LN:SADNAS55][AC:X87104] [GN:mdr] [FN:multiple grug resistance] [OR:Staphylococcusaureus] 104 SPX0701 701 3362 180 540 179 9.60E-18 [LN:S58356][AC:S66651:S58356] [PN:pepT protein] [GN:pepT] [CL:unassignedATP-binding cassette proteins:ATP-binding cassette homology][OR:Staphylococcus epidermidis] 166 SPX0702 702 3363 182 546 4444.80E-55 [GI:1262136] [LN:SAPBP4GEN] [AC:X91786] [PN:ATP-bindingcassette transporter A] [GN:abcA] [OR:Staphylococcus aureus] 116 SPX0703703 3364 365 1095 681 2.80E-123 [LN:A69847] [AC:A69847][PN:cystathionine gamma-synthase homolog yjcI] [GN:yjcI][CL:O-succinylhomoserine (thiol)-lyase] [OR:Bacillus subtilis] 143SPX0704 704 3365 389 1167 582 1.60E-99 [LN:PATB_BACSU] [AC:Q08432][GN:PATB] [OR:Bacillus subtilis] [EC:2.6.1.-] [DE:PUTATIVEAMINOTRANSFERASE B,] [SP:Q08432] 121 SPX0705 705 3366 1033 3099 5521.00E-129 [GI:1769947] [LN:BCX98455] [AC:X98455] [GN:SNF] [OR:Bacilluscereus] 68 SPX0706 706 3367 206 618 NO-HIT 6 SPX0707 707 3368 445 1335491 2.00E-154 [LN:MURC_BACSU] [AC:P40778] [GN:MURC] [OR:Bacillussubtilis] [EC:6.3.2.8] [DE:ACETYLMURANOYL-L-ALANINE SYNTHETASE)][SP:P40778] 127 SPX0708 708 3369 155 465 NO-HIT 6 SPX0709 709 3370 119357 56 7.70E-05 [LN:A64491] [AC:A64491] [PN:N-terminal acetyltransferasecomplex, subunit ARD1 homolog] [CL:Escherichia coliribosomal-protein-alanine N-acetyltransferase rimI] [OR:Methanococcusjannaschii] 192 SPX0710 710 3371 71 213 NO-HIT 6 SPX0711 711 3372 5021506 185 2.10E-43 [LN:E69979] [AC:E69979] [PN:folate metabolism homologyrrL] [GN:yrrL] [CL:yceG protein] [OR:Bacillus subtilis] 110 SPX0712 7123373 161 483 271 3.60E-55 [LN:GREA_BACSU] [AC:P80240] [GN:GREA][OR:Bacillus subtilis] [DE:GREA) (GENERAL STRESS PROTEIN 20M) (GSP20M)][SP:P80240] 121 SPX0713 713 3374 61 183 121 2.50E-12 [LN:T30285][AC:T30285] [PN:hypothetical protein] [OR:Streptococcus pneumoniae] 79SPX0714 714 3375 163 489 152 1.50E-24 [LN:S31638] [AC:S31638][PN:hypothetical protein] [OR:Lactobacillus curvatus] 77 SPX0715 7153376 66 198 NO-HIT 6 SPX0716 716 3377 70 210 89 0.0001 [GI:4966270][LN:CELK09H11] [AC:U97002] [GN:K09H11.1] [OR:Caenorhabditis elegans] 81SPX0717 717 3378 148 444 419 7.50E-56 [GI:517210] [LN:SPU11799][AC:U11799] [OR:Streptococcus pyogenes] 65 SPX0718 718 3379 164 492 4841.40E-63 [GI:517210] [LN:SPU11799] [AC:U11799] [OR:Streptococcuspyogenes] 65 SPX0719 719 3380 67 201 331 3.00E-44 [LN:S49404][AC:S49404:S38206] [PN:H+-transporting ATP synthase, chain c] [GN:atpC][CL:H+-transporting ATP synthase lipid-binding protein][OR:Streptococcus pneumoniae] [EC:3.6.1.34] 185 SPX0720 720 3381 239 7171205 5.00E-168 [LN:ATP6_STRPN] [AC:Q59954] [GN:ATPB:ATPA][OR:Streptococcus pneumoniae] [EC:3.6.1.34] [DE:ATP SYNTHASE A CHAIN,(PROTEIN 6)] [SP:Q59954] 139 SPX0721 721 3382 165 495 769 2.90E-100[LN:ATPF_STRPN] [AC:Q59952:Q59955] [GN:ATPF:ATPB] [OR:Streptococcuspneumoniae] [EC:3.6.1.34] [DE:ATP SYNTHASE B CHAIN, (SUBUNIT I)][SP:Q59952:Q59955] 153 SPX0722 722 3383 179 537 509 8.40E-66[GI:4100654] [LN:AF001955] [AC:AF001955] [PN:proton-translocating ATPasedelta subunit] [GN:uncH] [OR:Streptococcus sanguinis] 126 SPX0723 7233384 502 1506 2347 0 [GI:4100655] [LN:AF001955] [AC:AF001955][PN:proton-translocating ATPase alpha subunit] [GN:uncA][OR:Streptococcus sanguinis] 126 SPX0724 724 3385 293 879 1011 1.70E-169[GI:4100656] [LN:AF001955] [AC:AF001955] [PN:proton-translocating ATPasegamma subunit] [OR:Streptococcus sanguinis] 116 SPX0725 725 3386 4691407 2287 0 [GI:4100657] [LN:AF001955] [AC:AF001955][PN:proton-translocating ATPase beta subunit] [GN:uncD][OR:Streptococcus sanguinis] 125 SPX0726 726 3387 140 420 581 1.40E-76[GI:4100658] [LN:AF001955] [AC:AF001955] [PN:proton-translocating ATPaseepsilon subunit] [GN:uncC] [OR:Streptococcus sanguinis] 128 SPX0727 7273388 251 753 175 2.70E-42 [GI:6746427] [LN:AF179847] [AC:AF179847][PN:putative transposase] [OR:Lactococcus lactis] 90 SPX0728 728 3389 65195 NO-HIT 6 SPX0729 729 3390 182 546 107 1.20E-15 [GI:3849798][LN:U91581] [AC:U91581:U04057] [PN:putative transposase] [GN:tpase][OR:Lactococcus lactis subsp. lactis] 118 SPX0730 730 3391 338 1014 4441.50E-117 [GI:3242228] [LN:LLCADHE] [AC:AJ001007] [GN:orfB][OR:Lactococcus lactis] 73 SPX0731 731 3392 78 234 NO-HIT 6 SPX0732 7323393 389 1167 1141 1.60E-158 [GI:4098497] [LN:SMU78604] [AC:U78604][PN:putative membrane protein] [OR:Streptococcus mutans] 95 SPX0733 7333394 410 1230 457 6.20E-71 [GI:473901] [LN:LACALS] [AC:L16975][OR:Lactococcus lactis] [SR:Lactococcus lactis (strain DSM 20384,sub_species lactis) DNA] 128 SPX0734 734 3395 214 642 351 1.70E-45[LN:A72357] [AC:A72357] [PN:amino acid ABC transporter, permeaseprotein] [GN:TM0592] [CL:histidine permease protein M] [OR:Thermotogamaritima] 146 SPX0735 735 3396 210 630 367 2.90E-65 [GI:1649037][LN:STU73111] [AC:U73111] [PN:glutamine transport ATP-binding proteinGLNQ] [OR:Salmonella typhimurium] 116 SPX0736 736 3397 279 837 14114.70E-188 [GI:5929889] [LN:AF165218] [AC:AF165218] [PN:AatB] [GN:aatB][OR:Streptococcus pneumoniae] 90 SPX0737 737 3398 116 348 578 1.80E-76[GI:5929888] [LN:AF165218] [AC:AF165218] [PN:Bta] [GN:bta][OR:Streptococcus pneumoniae] 88 SPX0738 738 3399 573 1719 2903 0[GI:5929887] [LN:AF165218] [AC:AF165218] [PN:Pgm] [GN:pgm][OR:Streptococcus pneumoniae] 88 SPX0739 739 3400 109 327 129 8.30E-12[GI:4200438] [LN:AF026471] [AC:AF026471] [PN:putative transposase][OR:Streptococcus pneumoniae] 96 SPX0740 740 3401 100 300 245 5.10E-30[GI:5019553] [LN:SPN239004] [AC:AJ239004] [PN:putative transposase][OR:Streptococcus pneumoniae] 97 SPX0741 741 3402 95 285 NO-HIT 6SPX0742 742 3403 85 255 NO-HIT 6 SPX0743 743 3404 71 213 NO-HIT 6SPX0744 744 3405 371 1113 NO-HIT 6 SPX0745 745 3406 174 522 72 1.10E-05[LN:I38170] [AC:I38170] [PN:gene hr44 protein] [GN:hr44] [OR:Homosapiens] [SR:, man] 87 SPX0746 746 3407 290 870 335 2.40E-72 [LN:B72254][AC:B72254] [PN:glycerol uptake facilitator protein] [GN:TM1429][CL:glycerol facilitator protein] [OR:Thermotoga maritima] 135 SPX0747747 3408 399 1197 2022 6.40E-273 [LN:EFTU_STROR] [AC:P33170] [GN:TUF][OR:Streptococcus oralis] [DE:ELONGATION FACTOR TU (EF-TU)] [SP:P33170]108 SPX0748 748 3409 128 384 104 1.80E-06 [LN:H71023] [AC:H71023][PN:hypothetical protein PH1485] [GN:PH1485] [OR:Pyrococcus horikoshii]95 SPX0749 749 3410 138 414 99 6.40E-06 [LN:S31840] [AC:S31840][PN:probable transposase] [OR:Bacillus stearothermophilus] 82 SPX0750750 3411 62 186 NO-HIT 6 SPX0751 751 3412 218 654 163 3.90E-21[GI:722339] [LN:AXU22323] [AC:U22323] [PN:unknown] [OR:Acetobacterxylinus] [SR:Acetobacter xylinum] 100 SPX0752 752 3413 361 1083 2722.20E-72 [LN:C69813] [AC:C69813] [PN:RNA helicase homolog yfmL][GN:yfmL] [CL:unassigned DEAD/H box helicases:DEAD/H box helicasehomology] [OR:Bacillus subtilis] 153 SPX0753 753 3414 354 1062 1973.10E-44 [LN:YGJR_ECOLI] [AC:P42599:P42600:P76661] [GN:YGJR][OR:Escherichia coli] [DE:HYPOTHETICAL 36.2 KD PROTEIN IN EBGC-UXAAINTERGENIC REGION] [SP:P42599:P42600:P76661] 164 SPX0754 754 3415 62 18677 0.00028 [LN:S67482] [AC:S67482:S52150] [PN:serineO-acetyltransferase,, cytosolic:serine acetyltransferase:serineacetyltransferase] [OR:Arabidopsis thaliana] 152 SPX0755 755 3416 126378 NO-HIT 6 SPX0756 756 3417 481 1443 485 5.60E-59 [LN:G69849][AC:G69849] [PN:endo-1,4-beta-xylanase homolog yjeA] [GN:yjeA] [CL:nodBhomology] [OR:Bacillus subtilis] 118 SPX0757 757 3418 256 768 3575.70E-83 [LN:C70040] [AC:C70040] [PN:plant-metabolite dehydrogenasehomolog yvgN] [GN:yvgN] [CL:aldehyde reductase] [OR:Bacillus subtilis]129 SPX0758 758 3419 77 231 NO-HIT 6 SPX0759 759 3420 254 762 NO-HIT 6SPX0760 760 3421 306 918 1187 3.50E-159 [LN:SYGA_BACSU] [AC:P54380][GN:GLYQ] [OR:Bacillus subtilis] [EC:6.1.1.14] [DE:ALPHA CHAIN) (GLYRS)][SP:P54380] 112 SPX0761 761 3422 679 2037 1334 6.50E-179 [LN:SYGB_BACSU][AC:P54381] [GN:GLYS] [OR:Bacillus subtilis] [EC:6.1.1.14] [DE:BETACHAIN) (GLYRS)] [SP:P54381] 111 SPX0762 762 3423 86 258 218 1.20E-24[LN:E69894] [AC:E69894] [PN:hypothetical protein ynzC] [GN:ynzC][OR:Bacillus subtilis] 87 SPX0763 763 3424 415 1245 97 5.10E-08[LN:YIEF_ECOLI] [AC:P31465] [GN:YIEF] [OR:Escherichia coli][DE:HYPOTHETICAL 20.4 KD PROTEIN IN TNAB-BGLB INTERGENIC REGION][SP:P31465] 136 SPX0764 764 3425 79 237 NO-HIT 6 SPX0765 765 3426 202606 110 2.80E-13 [LN:YIEF_ECOLI] [AC:P31465] [GN:YIEF] [OR:Escherichiacoli] [DE:HYPOTHETICAL 20.4 KD PROTEIN IN TNAB-BGLB INTERGENIC REGION][SP:P31465] 136 SPX0766 766 3427 308 924 172 3.10E-41 [LN:APBE_TREPA][AC:O83774] [GN:APBE:TP0796] [OR:Treponema pallidum] [DE:THIAMINEBIOSYNTHESIS LIPOPROTEIN APBE PRECURSOR] [SP:O83774] 134 SPX0767 7673428 91 273 NO-HIT 6 SPX0768 768 3429 460 1380 2342 0 [GI:4416519][LN:AF014458] [AC:AF014458] [PN:NADH oxidase] [OR:Streptococcuspneumoniae] 88 SPX0769 769 3430 298 894 1411 3.40E-191 [LN:YG47_HAEIN][AC:P45293] [GN:HI1647] [OR:Haemophilus influenzae] [DE:HYPOTHETICALPROTEIN HI1647] [SP:P45293] 112 SPX0770 770 3431 78 234 125 3.00E-12[LN:F71007] [AC:F71007] [PN:hypothetical protein PH1356] [GN:PH1356][CL:Pyrococcus horikoshii hypothetical protein PH1356] [OR:Pyrococcushorikoshii] 150 SPX0771 771 3432 63 189 157 1.20E-15 [LN:F72782][AC:F72782] [PN:hypothetical protein APE0247] [GN:APE0247] [OR:Aeropyrumpernix] 92 SPX0772 772 3433 52 156 159 4.30E-16 [LN:F72782] [AC:F72782][PN:hypothetical protein APE0247] [GN:APE0247] [OR:Aeropyrum pernix] 92SPX0773 773 3434 194 582 720 2.40E-95 [LN:YG48_HAEIN] [AC:P45294][GN:HI1648] [OR:Haemophilus influenzae] [DE:HYPOTHETICAL PROTEIN HI1648][SP:P45294] 112 SPX0774 774 3435 216 648 183 5.00E-34 [LN:YA37_TREPA][AC:O84000] [GN:TP1037] [OR:Treponema pallidum] [DE:HYPOTHETICAL PROTEINTP1037] [SP:O84000] 108 SPX0775 775 3436 151 453 NO-HIT 6 SPX0776 7763437 165 495 94 2.80E-12 [LN:G81269] [AC:G81269] [PN:probableacetyltransferase Cj1715 [imported]] [GN:Cj1715] [OR:Campylobacterjejuni] 111 SPX0777 777 3438 177 531 167 1.80E-29 [GI:3694956][LN:AF091508] [AC:AF091508] [PN:O-6-methylguanine DNA methyltransferase][GN:ogt] [OR:Salmonella muenster] 119 SPX0778 778 3439 119 357 2722.10E-32 [LN:B70021] [AC:B70021] [PN:arsenate reductase homolog yusI][GN:yusI] [CL:hypothetical protein yjbD] [OR:Bacillus subtilis] 124SPX0779 779 3440 126 378 NO-HIT 6 SPX0780 780 3441 267 801 284 2.10E-54[LN:YXEN_BACSU] [AC:P54953] [GN:YXEN:LP9F] [OR:Bacillus subtilis][DE:INTERGENIC REGION] [SP:P54953] 100 SPX0781 781 3442 248 744 4685.80E-82 [GI:666983] [LN:BSPAAT] [AC:X77636] [PN:putative ATP bindingsubunit] [GN:ORF3] [OR:Bacillus subtilis] 102 SPX0782 782 3443 79 237NO-HIT 6 SPX0783 783 3444 74 222 NO-HIT 6 SPX0784 784 3445 266 798 5424.60E-98 [LN:TRXB_LISMO] [AC:O32823] [GN:TRXB] [OR:Listeriamonocytogenes] [EC:1.6.4.5] [DE:THIOREDOXIN REDUCTASE,] [SP:O32823] 120SPX0785 785 3446 254 762 322 1.30E-58 [LN:YACO_BACSU] [AC:Q06753][GN:YACO] [OR:Bacillus subtilis] [EC:2.1.1.-] [DE:HYPOTHETICAL TRNA/RRNAMETHYLTRANSFERASE YACO,] [SP:Q06753] 139 SPX0786 786 3447 204 612 3944.10E-93 [GI:806487] [LN:LACLPAGAP] [AC:L36907] [FN:unknown][OR:Lactococcus lactis] [SR:Lactococcus lactis (individual_isolateLM0230, sub_specie] 140 SPX0787 787 3448 84 252 NO-HIT 6 SPX0788 7883449 161 483 136 6.00E-14 [LN:H70069] [AC:H70069:JC7099][PN:poly-gamma-glutamic synthesis PgsA protein] [GN:ywtB:pgsA][OR:Bacillus subtilis] 116 SPX0789 789 3450 126 378 NO-HIT 6 SPX0790 7903451 276 828 242 8.80E-42 [LN:F64819] [AC:F64819] [PN:hypotheticalprotein b0822] [CL:Methanobacterium thermoautotrophicum conservedhypothetical protein MTH1071] [OR:Escherichia coli] 158 SPX0791 791 3452212 636 NO-HIT 6 SPX0792 792 3453 242 726 1196 1.80E-160 [GI:5001711][LN:AF112358] [AC:AF112358] [PN:C3-degrading proteinase] [GN:cppA][OR:Streptococcus pneumoniae] 109 SPX0793 793 3454 312 936 117 4.00E-22[GI:6469268] [LN:SCC75A] [AC:AL133220] [PN:possible secreted esterase][GN:SCC75A.29c] [OR:Streptomyces coelicolor A3(2)] 121 SPX0794 794 3455299 897 487 1.00E-64 [LN:YICL_ECOLI] [AC:P31437] [GN:YICL][OR:Escherichia coli] [DE:HYPOTHETICAL 33.1 KD PROTEIN IN SELC-NLPAINTERGENIC REGION] [SP:P31437] 136 SPX0795 795 3456 233 699 294 7.80E-49[LN:D70044] [AC:D70044] [PN:transcription regulator GntR family homologyvoA] [GN:yvoA] [CL:transcription regulator GntR] [OR:Bacillus subtilis]144 SPX0796 796 3457 521 1563 1721 3.40E-294 [GI:4321715] [LN:AF058326][AC:AF058326] [PN:GMP synthase] [GN:guaA] [OR:Lactococcus lactis] 92SPX0797 797 3458 62 186 NO-HIT 6 SPX0798 798 3459 96 288 204 2.90E-23[LN:JC1151] [AC:JC1151] [PN:hypothetical protein, 20.3K][OR:Agrobacterium tumefaciens] 89 SPX0799 799 3460 65 195 NO-HIT 6SPX0800 800 3461 130 390 91 0.00062 [GI:5824139] [LN:POL245436][AC:AJ245436:J04618:J04619:S50571:X52935:X65936] [PN:hypotheticalprotein, 57.8 kD] [OR:Pseudomonas putida] 137 SPX0801 801 3462 143 42984 9.20E-08 [GI:6009407] [LN:AB024946] [AC:AB024946] [GN:orf31][OR:Escherichia coli] [SR:Escherichia coli(sub_species:enteropathogenic, strain:B171] 140 SPX0802 802 3463 150 45094 3.20E-15 [LN:Y4HP_RHISN] [AC:P50360] [GN:Y4HP] [OR:Rhizobium sp][SR:,strain NGR234] [DE:HYPOTHETICAL 61.7 KD PROTEIN Y4HP] [SP:P50360]128 SPX0803 803 3464 78 234 87 0.00033 [GI:5824139] [LN:POL245436][AC:AJ245436:J04618:J04619:S50571:X52935:X65936] [PN:hypotheticalprotein, 57.8 kD] [OR:Pseudomonas putida] 137 SPX0804 804 3465 455 1365253 2.70E-62 [LN:D69159] [AC:D69159] [PN:methyl coenzyme M reductasesystem, component A2 homolog] [GN:MTH454] [CL:unassigned ATP-bindingcassette proteins:ATP-binding cassette homology] [OR:Methanobacteriumthermoautotrophicum] 217 SPX0805 805 3466 74 222 NO-HIT 6 SPX0806 8063467 232 696 88 1.90E-07 [LN:E72202] [AC:E72202] [PN:conservedhypothetical protein] [GN:TM1868] [OR:Thermotoga maritima] 96 SPX0807807 3468 195 585 NO-HIT 6 SPX0808 808 3469 582 1746 554 3.00E-83[GI:4097162] [LN:PMU46488] [AC:U46488] [PN:NrpB] [GN:nrpB] [OR:Proteusmirabilis] 81 SPX0809 809 3470 587 1761 526 2.60E-78 [GI:4097161][LN:PMU46488] [AC:U46488] [PN:NrpA] [GN:nrpA] [OR:Proteus mirabilis] 81SPX0810 810 3471 159 477 131 3.30E-12 [LN:SOXS_ECOLI] [AC:P22539][GN:SOXS] [OR:Escherichia coli] [DE:REGULATORY PROTEIN SOXS] [SP:P22539]100 SPX0811 811 3472 69 207 NO-HIT 6 SPX0812 812 3473 397 1191 8892.70E-126 [GI:2995646] [LN:AF051092] [AC:AF051092] [PN:DNA modificationmethyltransferase M.XbaI] [GN:xbaIM] [FN:recognizes ds DNA sequenceTCTAGA; thought to] [OR:Xanthomonas campestris] 177 SPX0813 813 3474 63189 128 1.30E-17 [GI:2995645] [LN:AF051092] [AC:AF051092][PN:restriction endonuclease R.XbaI] [GN:xbaIR] [FN:recognizes ds DNAsequence TCTAGA; cleaves both] [OR:Xanthomonas campestris] 169 SPX0814814 3475 61 183 199 4.80E-22 [GI:2995645] [LN:AF051092] [AC:AF051092][PN:restriction endonuclease R.XbaI] [GN:xbaIR] [FN:recognizes ds DNAsequence TCTAGA; cleaves both] [OR:Xanthomonas campestris] 169 SPX0815815 3476 71 213 NO-HIT 6 SPX0816 816 3477 429 1287 681 4.70E-147[LN:H69979] [AC:H69979] [PN:proteinase homolog yrrO] [GN:yrrO][CL:collagenase prtC] [OR:Bacillus subtilis] 107 SPX0817 817 3478 243729 251 6.20E-58 [LN:H69979] [AC:H69979] [PN:proteinase homolog yrrO][GN:yrrO] [CL:collagenase prtC] [OR:Bacillus subtilis] 107 SPX0818 8183479 241 723 225 4.40E-26 [LN:YCBN_BACSU] [AC:P42246] [GN:YCBN][OR:Bacillus subtilis] [DE:HYPOTHETICAL 31.7 KD PROTEIN IN GLTP-CWLJINTERGENIC REGION (ORF13)] [SP:P42246] 145 SPX0819 819 3480 243 729NO-HIT 6 SPX0820 820 3481 80 240 152 2.50E-16 [GI:1536960] [LN:SOORFS][AC:Z79691] [GN:yorfE] [FN:putative transcription regulator][OR:Streptococcus pneumoniae] 115 SPX0821 821 3482 163 489 NO-HIT 6SPX0822 822 3483 487 1461 981 1.70E-215 [LN:D70008] [AC:D70008][PN:nicotinate phosphoribosyltransferase homolog yueK] [GN:yueK][OR:Bacillus subtilis] 111 SPX0823 823 3484 275 825 923 1.70E-122[LN:NADE_ECOLI] [AC:P18843:P78235] [GN:NADE:EFG:NTRL] [OR:Escherichiacoli] [EC:6.3.5.1] [DE:PROTEIN)] [SP:P18843:P78235] 121 SPX0824 824 348566 198 NO-HIT 6 SPX0825 825 3486 184 552 135 1.80E-13 [GI:7635982][LN:SCE6] [AC:AL353832] [PN:putative acetyltransferase.] [GN:SCE6.13][OR:Streptomyces coelicolor A3(2)] 117 SPX0826 826 3487 250 750 660.00023 [GI:4185565] [LN:AF115379] [AC:AF115379] [PN:surface proteinPls] [GN:pls] [OR:Staphylococcus aureus] 101 SPX0827 827 3488 130 390306 1.70E-36 [LN:A41971] [AC:A41971:A60282:A33134] [PN:surface proteinpspA precursor:pneumococcal surface protein A] [GN:pspA] [CL:cpl repeathomology] [OR:Streptococcus pneumoniae] 169 SPX0828 828 3489 347 10411229 5.30E-166 [LN:QUEA_BACSU] [AC:O32054] [GN:QUEA] [OR:Bacillussubtilis] [EC:5.-.-.-] [DE:(QUEUOSINE BIOSYNTHESIS PROTEIN QUEA)][SP:O32054] 128 SPX0829 829 3490 236 708 336 3.00E-66 [LN:NAGB_BACSU][AC:O35000] [GN:NAGB] [OR:Bacillus subtilis] [EC:5.3.1.10] [DE:PHOSPHATEDEAMINASE) (GNPDA) (GLCN6P DEAMINASE)] [SP:O35000] 139 SPX0830 830 349167 201 248 1.00E-29 [LN:T43742] [AC:T43742] [PN:ribosomal protein S21[imported]] [OR:Listeria monocytogenes] 89 SPX0831 831 3492 313 939 12247.60E-165 [GI:4884536] [LN:AB027460] [AC:AB027460] [PN:Hpr kinase][OR:Streptococcus bovis] [SR:Streptococcus bovis (strain:JB1) DNA] 123SPX0832 832 3493 192 576 608 1.30E-84 [LN:T11569] [AC:T11569][PN:prolipoprotein diacylglyceryl transferase,] [GN:lgt][CL:prolipoprotein diacylglyceryl transferase] [OR:Streptococcus mutans][EC:2.4.99.-] 169 SPX0833 833 3494 128 384 333 1.50E-41 [LN:T11570][AC:T11570] [PN:hypothetical protein 1] [OR:Streptococcus mutans] 77SPX0834 834 3495 110 330 NO-HIT 6 SPX0835 835 3496 130 390 164 5.70E-17[LN:T11571] [AC:T11571] [PN:hypothetical protein 2] [OR:Streptococcusmutans] 77 SPX0836 836 3497 377 1131 596 4.30E-126 [LN:B69640][AC:B69640] [PN:coproporphyrinogen oxidase, III, oxygen-independenthemN] [GN:hemN] [CL:oxygen-independent coproporphyrinogen oxidase][OR:Bacillus subtilis] [EC:1.3.3.3] 184 SPX0837 837 3498 166 498 NO-HIT6 SPX0838 838 3499 246 738 96 7.20E-11 [GI:4704640] [LN:AF110462][AC:AF110462] [PN:oleoyl-ACP thioesterase] [OR:Elaeis guineensis] 92SPX0839 839 3500 203 609 466 3.10E-59 [LN:H70023] [AC:H70023][PN:N-acetyl-glucosamine catabolism homolog yutF] [GN:yutF] [CL:nagDprotein] [OR:Bacillus subtilis] 124 SPX0840 840 3501 217 651 NO-HIT 6SPX0841 841 3502 108 324 NO-HIT 6 SPX0842 842 3503 134 402 447 5.60E-58[LN:D69843] [AC:D69843] [PN:conserved hypothetical protein yjbD][GN:yjbD] [CL:hypothetical protein yjbD] [OR:Bacillus subtilis] 128SPX0843 843 3504 93 279 216 2.40E-24 [LN:C69864] [AC:C69864][PN:hypothetical protein yktA] [GN:yktA] [OR:Bacillus subtilis] 87SPX0844 844 3505 283 849 207 1.30E-46 [LN:SUHB_BACSU] [AC:Q45499][GN:SUHB] [OR:Bacillus subtilis] [DE:EXTRAGENIC SUPPRESSOR PROTEIN SUHBHOMOLOG] [SP:Q45499] 120 SPX0845 845 3506 113 339 NO-HIT 6 SPX0846 8463507 305 915 143 8.30E-21 [LN:YEBU_ECOLI] [AC:P76273:O07980] [GN:YEBU][OR:Escherichia coli] [DE:HYPOTHETICAL 53.2 KD PROTEIN IN PRC-PRPAINTERGENIC REGION] [SP:P76273:O07980] 149 SPX0847 847 3508 76 228 NO-HIT6 SPX0848 848 3509 56 168 NO-HIT 6 SPX0849 849 3510 78 234 NO-HIT 6SPX0850 850 3511 293 879 465 1.40E-80 [LN:YQGG_BACSU] [AC:P46338][GN:YQGG] [OR:Bacillus subtilis] [DE:REGION PRECURSOR (ORF108)][SP:P46338] 103 SPX0851 851 3512 306 918 403 1.00E-99 [LN:YQGH_BACSU][AC:P46339] [GN:YQGH] [OR:Bacillus subtilis] [DE:REGION (ORF72)][SP:P46339] 92 SPX0852 852 3513 295 885 842 2.80E-114 [LN:YQGI_BACSU][AC:P46340] [GN:YQGI] [OR:Bacillus subtilis] [DE:REGION (ORF73)][SP:P46340] 92 SPX0853 853 3514 268 804 796 1.10E-105 [LN:PSTB_METJA][AC:Q58418] [GN:PSTB:MJ1012] [OR:Methanococcus jannaschii] [DE:PROBABLEPHOSPHATE TRANSPORT ATP-BINDING PROTEIN PSTB] [SP:Q58418] 145 SPX0854854 3515 253 759 763 7.10E-100 [LN:T43868] [AC:T43868] [PN:phosphatetransport system peripheral membrane protein B [imported]] [GN:pstB][CL:inner membrane protein malK:ATP-binding cassette homology][OR:Pseudomonas putida] 193 SPX0855 855 3516 218 654 212 3.70E-40[GI:4530451] [LN:AF118229] [AC:AF118229] [PN:PhoU] [GN:phoU][OR:Streptococcus pneumoniae] 90 SPX0856 856 3517 272 816 190 2.40E-30[LN:B72357] [AC:B72357] [PN:amino acid ABC transporter, periplasmicamino acid-binding protein] [GN:TM0593][CL:lysine-arginine-ornithine-binding protein] [OR:Thermotoga maritima]181 SPX0857 857 3518 424 1272 778 4.20E-129 [GI:4580622] [LN:AF118389][AC:AF118389] [PN:unknown] [OR:Streptococcus suis] 77 SPX0858 858 351957 171 NO-HIT 6 SPX0859 859 3520 171 513 340 3.10E-77 [GI:1524117][LN:LLALDB] [AC:X82620] [PN:alpha-acetolactate decarboxylase] [GN:aldB][OR:Lactococcus lactis] 108 SPX0860 860 3521 67 201 265 2.40E-33[GI:1808671] [LN:SGCSHAG] [AC:X65164:S52427] [PN:putativealpha-acetolactate decarboxylase] [GN:aldB] [OR:Streptococcus gordonii]129 SPX0861 861 3522 243 729 106 1.50E-25 [LN:A69830] [AC:A69830][PN:hypothetical protein yhfC] [GN:yhfC] [OR:Bacillus subtilis] 87SPX0862 862 3523 302 906 212 5.60E-55 [LN:MURB_BACSU][AC:P18579:P16669:P37581] [GN:MURB] [OR:Bacillus subtilis][EC:1.1.1.158] [DE:ACETYLMURAMATE DEHYDROGENASE)][SP:P18579:P16669:P37581] 150 SPX0863 863 3524 379 1137 792 1.80E-114[LN:A70180] [AC:A70180] [PN:spermidine/putrescine ABC transporter,ATP-binding protein (potA) homolog] [CL:unassigned ATP-binding cassetteproteins:ATP-binding cassette homology] [OR:Borrelia burgdorferi] [SR:,Lyme disease spirochete] 237 SPX0864 864 3525 109 327 NO-HIT 6 SPX0865865 3526 211 633 324 4.20E-44 [LN:H70179] [AC:H70179][PN:spermidine/putrescine ABC transporter, permease protein (potB)homolog] [CL:spermidine/putrescine transport system permease proteinpotH] [OR:Borrelia burgdorferi] [SR:, Lyme disease spirochete] 224SPX0866 866 3527 258 774 346 7.00E-66 [LN:G70179] [AC:G70179][PN:spermidine/putrescine ABC transporter, permease protein (potC)homolog] [CL:spermidine/putrescine transport system permease proteinpotI] [OR:Borrelia burgdorferi] [SR:, Lyme disease spirochete] 224SPX0867 867 3528 226 678 173 5.20E-48 [LN:POTD_ECOLI] [AC:P23861][GN:POTD] [OR:Escherichia coli] [DE:SPERMIDINE/PUTRESCINE-BINDINGPERIPLASMIC PROTEIN PRECURSOR (SPBP)] [SP:P23861] 143 SPX0868 868 3529125 375 197 1.30E-20 [LN:POTD_ECOLI] [AC:P23861] [GN:POTD][OR:Escherichia coli] [DE:SPERMIDINE/PUTRESCINE-BINDING PERIPLASMICPROTEIN PRECURSOR (SPBP)] [SP:P23861] 143 SPX0869 869 3530 80 240 NO-HIT6 SPX0870 870 3531 73 219 NO-HIT 6 SPX0871 871 3532 163 489 159 4.70E-15[LN:G70079] [AC:G70079] [PN:hypothetical protein yxjI] [GN:yxjI][CL:Bacillus subtilis hypothetical protein yxjI] [OR:Bacillus subtilis]136 SPX0872 872 3533 89 267 332 2.40E-39 [LN:SYA_BACSU] [AC:O34526][GN:ALAS] [OR:Bacillus subtilis] [EC:6.1.1.7] [DE:ALANYL-TRNASYNTHETASE, (ALANINE--TRNA LIGASE) (ALARS)] [SP:O34526] 146 SPX0873 8733534 787 2361 570 1.20E-202 [LN:SYA_BACSU] [AC:O34526] [GN:ALAS][OR:Bacillus subtilis] [EC:6.1.1.7] [DE:ALANYL-TRNA SYNTHETASE,(ALANINE--TRNA LIGASE) (ALARS)] [SP:O34526] 146 SPX0874 874 3535 4851455 1726 2.50E-257 [GI:2760119] [LN:AB000830] [AC:AB000830][PN:alpha-amylase precursor] [OR:Streptococcus bovis] [SR:Streptococcusbovis (strain:148) DNA] 136 SPX0875 875 3536 64 192 NO-HIT 6 SPX0876 8763537 250 750 489 1.10E-62 [LN:H75077] [AC:H75077] [PN:abc transporter,ATP-binding protein PAB1696] [GN:PAB1696] [CL:unassigned ATP-bindingcassette proteins:ATP-binding cassette homology] [OR:Pyrococcus abyssi]187 SPX0877 877 3538 545 1635 NO-HIT 6 SPX0878 878 3539 388 1164 4682.20E-96 [LN:YWBD_BACSU] [AC:P39587] [GN:YWBD:IPA-19D] [OR:Bacillussubtilis] [DE:HYPOTHETICAL 44.4 KD PROTEIN IN EPR-GALK INTERGENICREGION] [SP:P39587] 144 SPX0879 879 3540 226 678 165 6.60E-27[GI:5919207] [LN:AF184963] [AC:AF184963] [PN:3-dehydroquinase] [GN:aroD][OR:Salmonella enteritidis] 100 SPX0880 880 3541 285 855 680 5.70E-89[GI:3821433] [LN:SPN232281] [AC:AJ232281] [PN:shikimate dehydrogenase][GN:aroE] [OR:Streptococcus pneumoniae] 110 SPX0881 881 3542 356 1068439 3.10E-84 [LN:AROB_SYNY3] [AC:P73997] [GN:AROB:SLR2130][OR:Synechocystis sp] [SR:,strain PCC 6803] [EC:4.6.1.3][DE:3-DEHYDROQUINATE SYNTHASE,] [SP:P73997] 148 SPX0882 882 3543 3891167 790 1.40E-142 [LN:AROC_BACSU] [AC:P31104] [GN:AROF] [OR:Bacillussubtilis] [EC:4.6.1.4] [DE:PHOSPHOLYASE) (VEGETATIVE PROTEIN 216)(VEG216)] [SP:P31104] 138 SPX0883 883 3544 368 1104 402 2.40E-127[LN:TYRA_LACLA] [AC:P43901] [GN:TYRA] [OR:Lactococcus lactis][SR:,subsplactis:Streptococcus lactis] [EC:1.3.1.12] [DE:PREPHENATEDEHYDROGENASE, (PDH)] [SP:P43901] 165 SPX0884 884 3545 113 339 1527.80E-16 [GI:3688819] [LN:AF084104] [AC:AF084104] [PN:hypotheticalprotein] [OR:Bacillus firmus] 87 SPX0885 885 3546 428 1284 20941.40E-284 [GI:5616525] [LN:AF169483] [AC:AF169483][PN:5-enolpyruvylshikimate-3-phosphate synthase] [GN:aroA][OR:Streptococcus pneumoniae] 129 SPX0886 886 3547 159 477 262 3.60E-40[LN:AROK_LACLA] [AC:P43906] [GN:AROK] [OR:Lactococcus lactis][SR:,subsplactis:Streptococcus lactis] [EC:2.7.1.71] [DE:SHIKIMATEKINASE, (SK)] [SP:P43906] 156 SPX0887 887 3548 282 846 707 3.20E-98[LN:PHEA_LACLA] [AC:P43909] [OR:Lactococcus lactis][SR:,subsplactis:Streptococcus lactis] [EC:4.2.1.51] [DE:PREPHENATEDEHYDRATASE, (PDT)] [SP:P43909] 153 SPX0888 888 3549 231 693 91 7.60E-09[GI:7160813] [LN:EFA276231] [AC:AJ276231] [PN:PSR protein] [GN:psr][FN:unknown] [OR:Enterococcus faecalis] 107 SPX0889 889 3550 200 600 2689.10E-46 [GI:7160813] [LN:EFA276231] [AC:AJ276231] [PN:PSR protein][GN:psr] [FN:unknown] [OR:Enterococcus faecalis] 107 SPX0890 890 3551282 846 172 1.10E-24 [LN:LICD_HAEIN] [AC:P14184] [GN:LICD][OR:Haemophilus influenzae] [DE:LICD PROTEIN] [SP:P14184] 95 SPX0891 8913552 134 402 NO-HIT 6 SPX0892 892 3553 386 1158 244 1.70E-28 [LN:F70441][AC:F70441] [PN:capsular polysaccharide biosynthsis protein] [GN:cap][OR:Aquifex aeolicus] 103 SPX0893 893 3554 329 987 327 4.10E-51[GI:3320393] [LN:AF030373] [AC:AF030373] [PN:galactosyl transferase][GN:cps23FU] [OR:Streptococcus pneumoniae] 111 SPX0894 894 3555 478 143496 0.00022 [GI:5931973] [LN:AF125164] [AC:AF125164] [PN:putativepolymerase] [GN:wzy] [OR:Bacteroides fragilis] 100 SPX0895 895 3556 151453 NO-HIT 6 SPX0896 896 3557 202 606 NO-HIT 6 SPX0897 897 3558 99 297NO-HIT 6 SPX0898 898 3559 185 555 349 1.10E-42 [GI:5360696][LN:AB022909] [AC:AB022909] [PN:negative regulator of geneticcompetence] [GN:mecA] [OR:Streptococcus mutans] [SR:Streptococcus mutans(strain:Xc) DNA] 164 SPX0899 899 3560 128 384 NO-HIT 6 SPX0900 900 356171 213 127 1.70E-11 [GI:5360696] [LN:AB022909] [AC:AB022909][PN:negative regulator of genetic competence] [GN:mecA][OR:Streptococcus mutans] [SR:Streptococcus mutans (strain:Xc) DNA] 164SPX0901 901 3562 429 1287 1425 2.60E-191 [LN:DHOM_LACLA] [AC:P52985][GN:HOM] [OR:Lactococcus lactis] [SR:,subsplactis:Streptococcus lactis][EC:1.1.1.3] [DE:HOMOSERINE DEHYDROGENASE, (HDH)] [SP:P52985] 163SPX0902 902 3563 290 870 1439 4.70E-194 [LN:KHSE_STRPN] [AC:P72535][GN:THRB] [OR:Streptococcus pneumoniae] [EC:2.7.1.39] [DE:HOMOSERINEKINASE, (HK)] [SP:P72535] 124 SPX0903 903 3564 142 426 NO-HIT 6 SPX0904904 3565 75 225 192 8.30E-23 [LN:T30285] [AC:T30285] [PN:hypotheticalprotein] [OR:Streptococcus pneumoniae] 79 SPX0905 905 3566 86 258 3666.80E-46 [LN:PMSR_STRPN] [AC:P35593] [GN:MSRA:EXP3] [OR:Streptococcuspneumoniae] [DE:(EXPORTED PROTEIN 3)] [SP:P35593] 110 SPX0906 906 3567256 768 1236 9.90E-167 [LN:PMSR_STRPN] [AC:P35593] [GN:MSRA:EXP3][OR:Streptococcus pneumoniae] [DE:(EXPORTED PROTEIN 3)] [SP:P35593] 110SPX0907 907 3568 103 309 123 6.70E-10 [LN:E72396] [AC:E72396] [PN:ABCtransporter, ATP-binding protein] [GN:TM0287] [CL:unassigned ATP-bindingcassette proteins:ATP-binding cassette homology] [OR:Thermotogamaritima] 180 SPX0908 908 3569 488 1464 472 3.40E-92 [LN:E72396][AC:E72396] [PN:ABC transporter, ATP-binding protein] [GN:TM0287][CL:unassigned ATP-binding cassette proteins:ATP-binding cassettehomology] [OR:Thermotoga maritima] 180 SPX0909 909 3570 62 186 NO-HIT 6SPX0910 910 3571 584 1752 722 7.90E-145 [LN:Y08A_MYCTU] [AC:Q11047][GN:MTCY50.10] [OR:Mycobacterium tuberculosis] [DE:HYPOTHETICAL ABCTRANSPORTER ATP-BINDING PROTEIN CY50.10] [SP:Q11047] 148 SPX0911 9113572 86 258 325 5.10E-41 [LN:T30285] [AC:T30285] [PN:hypotheticalprotein] [OR:Streptococcus pneumoniae] 79 SPX0912 912 3573 129 387 958.00E-06 [LN:T30285] [AC:T30285] [PN:hypothetical protein][OR:Streptococcus pneumoniae] 79 SPX0913 913 3574 64 192 NO-HIT 6SPX0914 914 3575 74 222 NO-HIT 6 SPX0915 915 3576 69 207 NO-HIT 6SPX0916 916 3577 65 195 NO-HIT 6 SPX0917 917 3578 99 297 NO-HIT 6SPX0918 918 3579 295 885 447 1.10E-56 [LN:A70039] [AC:A70039] [PN:ABCtransporter (ATP-binding protein) homolog yvfR] [GN:yvfR] [CL:unassignedATP-binding cassette proteins:ATP-binding cassette homology][OR:Bacillus subtilis] 188 SPX0919 919 3580 246 738 289 1.00E-39[GI:6759480] [LN:BCE243712] [AC:AJ243712] [PN:YVFS protein] [GN:yvfS][OR:Bacillus cereus] 90 SPX0920 920 3581 366 1098 1715 5.40E-238[GI:5830547] [LN:SPAJ6400] [AC:AJ006400] [PN:histidine kinase] [GN:hk11][OR:Streptococcus pneumoniae] 102 SPX0921 921 3582 200 600 932 2.00E-123[GI:5830548] [LN:SPAJ6400] [AC:AJ006400] [PN:response regulator][GN:rr11] [OR:Streptococcus pneumoniae] 104 SPX0922 922 3583 337 10111328 1.10E-176 [GI:7328454] [LN:AB028599] [AC:AB028599] [PN:catabolitecontrol protein A] [GN:ccpA] [OR:Streptococcus bovis] [SR:Streptococcusbovis (strain:JB1) DNA] 151 SPX0923 923 3584 131 393 270 4.60E-32[LN:T30285] [AC:T30285] [PN:hypothetical protein] [OR:Streptococcuspneumoniae] 79 SPX0924 924 3585 113 339 89 5.70E-05 [LN:T30285][AC:T30285] [PN:hypothetical protein] [OR:Streptococcus pneumoniae] 79SPX0925 925 3586 321 963 295 8.70E-56 [LN:G75283] [AC:G75283][PN:L-asparaginase] [GN:DR2353] [CL:asparaginase] [OR:Deinococcusradiodurans] 102 SPX0926 926 3587 463 1389 213 9.90E-43 [LN:C69862][AC:C69862] [PN:conserved hypothetical protein ykrA] [GN:ykrA][CL:Methanobacterium thermoautotrophicum conserved hypothetical proteinMTH1071] [OR:Bacillus subtilis] 178 SPX0927 927 3588 151 453 1276.20E-14 [LN:A69220] [AC:A69220] [PN:conserved hypothetical proteinMTH898] [GN:MTH898] [CL:Escherichia coli ybdQ protein][OR:Methanobacterium thermoautotrophicum] 155 SPX0928 928 3589 97 291NO-HIT 6 SPX0929 929 3590 239 717 819 4.70E-109 [LN:YFBQ_HAEIN][AC:P71348] [GN:HI0286] [OR:Haemophilus influenzae] [EC:2.6.1.-][DE:PROBABLE AMINOTRANSFERASE HI0286,] [SP:P71348] 133 SPX0930 930 3591111 333 NO-HIT 6 SPX0931 931 3592 125 375 385 1.70E-48 [LN:YFBQ_HAEIN][AC:P71348] [GN:HI0286] [OR:Haemophilus influenzae] [EC:2.6.1.-][DE:PROBABLE AMINOTRANSFERASE HI0286,] [SP:P71348] 133 SPX0932 932 359345 135 170 7.60E-20 [LN:RL34_BACST] [AC:P23376] [GN:RPMH] [OR:Bacillusstearothermophilus] [DE:50S RIBOSOMAL PROTEIN L34] [SP:P23376] 113SPX0933 933 3594 67 201 NO-HIT 6 SPX0934 934 3595 218 654 116 9.60E-07[GI:546643] [LN:S70345] [AC:S70345] [PN:SpaA] [GN:SpaA][OR:Streptococcus sobrinus] [SR:Streptococcus sobrinus MUCOB 263] 121SPX0935 935 3596 75 225 180 6.20E-19 [LN:YABD_BACSU] [AC:P37545][GN:YABD] [OR:Bacillus subtilis] [DE:HYPOTHETICAL 29.2 KD PROTEIN INMETS-KSGA INTERGENIC REGION] [SP:P37545] 137 SPX0936 936 3597 181 543469 3.60E-60 [LN:YABD_BACSU] [AC:P37545] [GN:YABD] [OR:Bacillussubtilis] [DE:HYPOTHETICAL 29.2 KD PROTEIN IN METS-KSGA INTERGENICREGION] [SP:P37545] 137 SPX0937 937 3598 187 561 235 2.70E-52[LN:YABF_BACSU] [AC:P37547] [GN:YABF] [OR:Bacillus subtilis][DE:HYPOTHETICAL 20.7 KD PROTEIN IN METS-KSGA INTERGENIC REGION][SP:P37547] 137 SPX0938 938 3599 304 912 NO-HIT 6 SPX0939 939 3600 99297 149 3.30E-15 [GI:7576923] [LN:AF242367] [AC:AF242367][PN:lactococcin 972] [GN:lclA] [OR:Lactococcus lactis subsp. lactis] 109SPX0940 940 3601 269 807 65 5.50E-08 [GI:3355783] [LN:LLJ002203][AC:AJ002203] [PN:putative immunity] [GN:orf2] [OR:Lactococcus lactis]98 SPX0941 941 3602 450 1350 357 1.30E-89 [GI:4009478] [LN:AF068902][AC:AF068902] [PN:unknown] [OR:Streptococcus pneumoniae] 83 SPX0942 9423603 214 642 667 2.50E-87 [GI:4009479] [LN:AF068902] [AC:AF068902][PN:unknown] [OR:Streptococcus pneumoniae] 83 SPX0943 943 3604 103 309NO-HIT 6 SPX0944 944 3605 169 507 NO-HIT 6 SPX0945 945 3606 291 873 7813.80E-104 [LN:KSGA_BACSU] [AC:P37468] [GN:KSGA] [OR:Bacillus subtilis][EC:2.1.1.-] [DE:DIMETHYLTRANSFERASE)] [SP:P37468] 111 SPX0946 946 3607293 879 394 5.10E-100 [LN:A69879] [AC:A69879] [PN:conserved hypotheticalprotein yloQ] [GN:yloQ] [CL:conserved hypothetical protein HI1714][OR:Bacillus subtilis] 140 SPX0947 947 3608 301 903 460 1.20E-69[LN:RPE_RHOCA] [AC:P51012] [GN:CBBE] [OR:Rhodobacter capsulatus][SR:,Rhodopseudomonas capsulata] [EC:5.1.3.1] [DE:EPIMERASE) (PPE)(R5P3E)] [SP:P51012] 154 SPX0948 948 3609 221 663 143 3.50E-18[LN:C69879] [AC:C69879] [PN:hypothetical protein yloS] [GN:yloS][OR:Bacillus subtilis] 87 SPX0949 949 3610 405 1215 91 5.10E-07[LN:E81528] [AC:E81528] [PN:conserved hypothetical protein CP0874[imported]] [GN:CP0874] [OR:Chlamydophila pneumoniae:Chlamydiapneumoniae] 140 SPX0950 950 3611 314 942 453 1.00E-88 [LN:G69818][AC:G69818] [PN:CMP-binding factor homolog yhaM] [GN:yhaM] [OR:Bacillussubtilis] 93 SPX0951 951 3612 276 828 498 2.80E-98 [GI:2706406][LN:LLAJ642] [AC:AJ222642] [GN:purR] [FN:activator of purinebiosynthetic genes] [OR:Lactococcus lactis] 117 SPX0952 952 3613 70 21083 0.00046 [LN:TABA_PSESZ] [AC:P31851] [GN:TABA] [OR:Pseudomonassyringae] [SR:,pvtabaci] [DE:TABA PROTEIN] [SP:P31851] 110 SPX0953 9533614 128 384 199 3.60E-21 [LN:TABA_PSESZ] [AC:P31851] [GN:TABA][OR:Pseudomonas syringae] [SR:,pvtabaci] [DE:TABA PROTEIN] [SP:P31851]110 SPX0954 954 3615 100 300 NO-HIT 6 SPX0955 955 3616 335 1005 3718.10E-63 [LN:TABA_PSESZ] [AC:P31851] [GN:TABA] [OR:Pseudomonas syringae][SR:,pvtabaci] [DE:TABA PROTEIN] [SP:P31851] 110 SPX0956 956 3617 265795 1121 8.40E-152 [LN:PFLA_STRMU] [AC:O68575] [GN:ACT:PFLC][OR:Streptococcus mutans] [EC:1.97.1.4] [DE:ENZYME)] [SP:O68575] 106SPX0957 957 3618 309 927 140 6.90E-32 [GI:6117974] [LN:AF139908][AC:AF139908] [PN:membrane protein homolog] [OR:Listeria monocytogenes]98 SPX0958 958 3619 93 279 108 9.80E-09 [LN:T35660] [AC:T35660][PN:probable acylphosphatase] [GN:SC7A1.20] [OR:Streptomyces coelicolor]96 SPX0959 959 3620 253 759 217 1.10E-43 [LN:G69984] [AC:G69984][PN:rRNA methylase homolog ysgA] [GN:ysgA] [CL:conserved hypotheticalprotein HI0860] [OR:Bacillus subtilis] 132 SPX0960 960 3621 228 684 4331.10E-57 [GI:3171165] [LN:AF064763] [AC:AF064763] [PN:putative membranespanning protein] [OR:Lactococcus lactis subsp. cremoris] 120 SPX0961961 3622 72 216 NO-HIT 6 SPX0962 962 3623 331 993 1387 1.70E-186[LN:ASNA_HAEIN] [AC:P44338] [GN:ASNA:HI0564] [OR:Haemophilus influenzae][EC:6.3.1.1] [DE:ASPARTATE--AMMONIA LIGASE, (ASPARAGINE SYNTHETASE A)][SP:P44338] 157 SPX0963 963 3624 180 540 279 1.30E-33 [LN:E69874][AC:E69874] [PN:conserved hypothetical protein ylbH] [GN:ylbH][CL:Escherichia coli hypothetical 21.7K protein (ftsY-nikA intergenicregion)] [OR:Bacillus subtilis] 176 SPX0964 964 3625 123 369 1843.00E-25 [LN:G81347] [AC:G81347] [PN:3-deoxy-D-manno-octulosonic-acidtransferase Cj0767c [imported]] [GN:kdtB:Cj0767c] [OR:Campylobacterjejuni] 136 SPX0965 965 3626 239 717 184 7.20E-17 [LN:A69875][AC:A69875] [PN:hypothetical protein ylbL] [GN:ylbL] [OR:Bacillussubtilis] 87 SPX0966 966 3627 78 234 101 1.90E-16 [LN:A69875][AC:A69875] [PN:hypothetical protein ylbL] [GN:ylbL] [OR:Bacillussubtilis] 87 SPX0967 967 3628 95 285 NO-HIT 6 SPX0968 968 3629 428 1284620 3.20E-133 [LN:MURA_ACICA] [AC:P33986] [GN:MURA:MURZ][OR:Acinetobacter calcoaceticus] [EC:2.5.1.7] [DE:TRANSFERASE) (EPT)][SP:P33986] 124 SPX0969 969 3630 75 225 320 4.60E-41 [LN:EPUA_STRPN][AC:Q03159] [GN:EPUA] [OR:Streptococcus pneumoniae] [DE:EPUA PROTEIN][SP:Q03159] 97 SPX0970 970 3631 275 825 1392 2.50E-182 [LN:NUCE_STRPN][AC:Q03158] [GN:ENDA] [OR:Streptococcus pneumoniae] [EC:3.1.30.-][DE:DNA-ENTRY NUCLEASE (COMPETENCE-SPECIFIC NUCLEASE),] [SP:Q03158] 151SPX0971 971 3632 328 984 1168 4.20E-160 [GI:2952527] [LN:AF051356][AC:AF051356] [PN:putative hemolysin] [GN:hlyX] [OR:Streptococcusmutans] 100 SPX0972 972 3633 95 285 266 6.50E-33 [GI:2952527][LN:AF051356] [AC:AF051356] [PN:putative hemolysin] [GN:hlyX][OR:Streptococcus mutans] 100 SPX0973 973 3634 1204 3612 1921 0[LN:T44375] [AC:T44375] [PN:rpoB protein [imported]] [CL:DNA-directedRNA polymerase beta chain] [OR:Bacillus halodurans] 121 SPX0974 974 3635116 348 NO-HIT 6 SPX0975 975 3636 57 171 NO-HIT 6 SPX0976 976 3637 12263678 4009 0 [LN:RPOC_STRPY] [AC:P95816] [GN:RPOC] [OR:Streptococcuspyogenes] [EC:2.7.7.6] [DE:BETA′CHAIN) (RNA POLYMERASE BETA′SUBUNIT)(FRAGMENT)] [SP:P95816] 150 SPX0977 977 3638 131 393 NO-HIT 6 SPX0978978 3639 138 414 192 4.30E-48 [GI:1655704] [LN:XLNM23] [AC:X97899][PN:NM23/nucleoside diphosphate kinase] [OR:Xenopus laevis] [SR:Africanclawed frog] 121 SPX0979 979 3640 93 279 NO-HIT 6 SPX0980 980 3641 211633 472 1.50E-87 [GI:4009479] [LN:AF068902] [AC:AF068902] [PN:unknown][OR:Streptococcus pneumoniae] 83 SPX0981 981 3642 672 2016 277 4.50E-70[GI:4009478] [LN:AF068902] [AC:AF068902] [PN:unknown] [OR:Streptococcuspneumoniae] 83 SPX0982 982 3643 65 195 NO-HIT 6 SPX0983 983 3644 288 864110 2.30E-09 [LN:JC6007] [AC:JC6007] [PN:transcription activator plcR][GN:plcR] [CL:Bacillus thuringiensis transcription activator plcR][OR:Bacillus thuringiensis] 152 SPX0984 984 3645 137 411 NO-HIT 6SPX0985 985 3646 159 477 166 2.20E-36 [LN:C69786] [AC:C69786][PN:conserved hypothetical protein ydiB] [GN:ydiB] [CL:hypotheticalprotein HI0065] [OR:Bacillus subtilis] 130 SPX0986 986 3647 173 519 1497.60E-28 [LN:D72360] [AC:D72360] [PN:conserved hypothetical protein][GN:TM0577] [OR:Thermotoga maritima] 96 SPX0987 987 3648 339 1017 1826.50E-46 [LN:LYTR_BACSU] [AC:Q02115] [GN:LYTR] [OR:Bacillus subtilis][DE:MEMBRANE-BOUND PROTEIN LYTR] [SP:Q02115] 105 SPX0988 988 3649 4191257 2015 1.70E-272 [LN:CINA_STRPN] [AC:P54184:Q54853] [GN:CINA:EXP10][OR:Streptococcus pneumoniae] [DE:PUTATIVE COMPETENCE-DAMAGE PROTEIN(EXPORTED PROTEIN 10)] [SP:P54184:Q54853] 161 SPX0989 989 3650 389 11671928 6.10E-256 [LN:RECA_STRPN] [AC:P30758] [GN:RECA] [OR:Streptococcuspneumoniae] [DE:RECA PROTEIN] [SP:P30758] 97 SPX0990 990 3651 457 13712252 0 [GI:2398825] [LN:SPCINREC] [AC:Z34303] [PN:DinF protein][GN:dinF] [OR:Streptococcus pneumoniae] 96 SPX0991 991 3652 319 957 17861.50E-240 [LN:ALYS_STRPN] [AC:P06653] [GN:LYTA] [OR:Streptococcuspneumoniae] [EC:3.5.1.28] [DE:HYDROLASE) (MUCOPEPTIDE AMINOHYDROLASE)(CELL WALL HYDROLASE)] [SP:P06653] 160 SPX0992 992 3653 79 237 NO-HIT 6SPX0993 993 3654 81 243 NO-HIT 6 SPX0994 994 3655 120 360 NO-HIT 6SPX0995 995 3656 142 426 NO-HIT 6 SPX0996 996 3657 75 225 NO-HIT 6SPX0997 997 3658 332 996 676 4.50E-129 [GI:2398827] [LN:SPCINREC][AC:Z34303] [PN:hypothetical protein] [OR:Streptococcus pneumoniae] 94SPX0998 998 3659 82 246 NO-HIT 6 SPX0999 999 3660 90 270 NO-HIT 6SPX1000 1000 3661 87 261 NO-HIT 6 SPX1001 1001 3662 101 303 296 7.00E-36[LN:S52544] [AC:S52544] [PN:ISL2 protein] [OR:Lactobacillus helveticus]71 SPX1002 1002 3663 44 132 108 5.70E-09 [LN:S52544] [AC:S52544][PN:ISL2 protein] [OR:Lactobacillus helveticus] 71 SPX1003 1003 3664 153459 NO-HIT 6 SPX1004 1004 3665 203 609 NO-HIT 6 SPX1005 1005 3666 137411 NO-HIT 6 SPX1006 1006 3667 472 1416 2426 0 [LN:A28568][AC:A28568:S12829] [PN:pneumolysin] [CL:dipeptide transport protein][OR:Streptococcus pneumoniae] 110 SPX1007 1007 3668 239 717 9151.30E-119 [LN:A64963] [AC:A64963] [PN:conserved hypothetical proteinb1983] [CL:hypothetical protein MG332] [OR:Escherichia coli] 119 SPX10081008 3669 150 450 104 9.20E-07 [LN:C72329] [AC:C72329] [PN:hypotheticalprotein TM0816] [GN:TM0816] [OR:Thermotoga maritima] 93 SPX1009 10093670 291 873 309 1.20E-35 [GI:6759558] [LN:SC7A8] [AC:AL137187][PN:putative ABC transporter] [GN:SC7A8.02] [OR:Streptomyces coelicolorA3(2)] 116 SPX1010 1010 3671 344 1032 335 7.80E-76 [GI:6759559][LN:SC7A8] [AC:AL137187] [PN:putative ABC transporter] [GN:SC7A8.03][OR:Streptomyces coelicolor A3(2)] 116 SPX1011 1011 3672 121 363 NO-HIT6 SPX1012 1012 3673 168 504 130 2.10E-10 [LN:Y374_METJA] [AC:Q57819][GN:MJ0374] [OR:Methanococcus jannaschii] [DE:HYPOTHETICAL PROTEINMJ0374] [SP:Q57819] 114 SPX1013 1013 3674 150 450 NO-HIT 6 SPX1014 10143675 225 675 NO-HIT 6 SPX1015 1015 3676 74 222 125 8.00E-13 [GI:1914870][LN:SPZ82001] [AC:Z82001] [PN:unknown] [OR:Streptococcus pneumoniae] 81SPX1016 1016 3677 100 300 NO-HIT 6 SPX1017 1017 3678 106 318 2766.70E-34 [LN:G69998] [AC:G69998] [PN:thioredoxin H1 homolog ytpP][GN:ytpP] [CL:thioredoxin:thioredoxin homology] [OR:Bacillus subtilis]127 SPX1018 1018 3679 126 378 NO-HIT 6 SPX1019 1019 3680 209 627 2175.30E-44 [LN:A69999] [AC:A69999] [PN:phenylalanyl-tRNA synthetase (betasubunit) homolog ytpR] [GN:ytpR] [CL:Mycoplasma genitalium hypotheticalprotein MG449] [OR:Bacillus subtilis] 172 SPX1020 1020 3681 254 762 3544.20E-67 [GI:2425123] [LN:AF019986] [AC:AF019986] [PN:PksB] [GN:pksB][OR:Dictyostelium discoideum] 90 SPX1021 1021 3682 132 396 227 1.20E-34[GI:6716352] [LN:AF145054] [AC:AF145054:AF001793:AF118440:U89246][PN:ORF9] [GN:orf9] [OR:Streptococcus thermophilus bacteriophage 7201]136 SPX1022 1022 3683 95 285 460 1.90E-58 [GI:4566772] [LN:AF117741][AC:AF117741] [PN:cochaperonin GroES] [GN:groES] [OR:Streptococcuspneumoniae] 105 SPX1023 1023 3684 203 609 344 8.20E-43 [GI:1196510][LN:MSGTCWPA] [AC:M15467] [PN:unknown protein] [OR:Mycobacteriumtuberculosis] [SR:Mycobacterium tuberculosis (strain Erdman) DNA] 143SPX1024 1024 3685 541 1623 2611 0 [GI:4566773] [LN:AF117741][AC:AF117741] [PN:chaperonin GroEL] [GN:groEL] [OR:Streptococcuspneumoniae] 103 SPX1025 1025 3686 70 210 70 3.30E-06 [LN:C71647][AC:C71647] [PN:hypothetical protein RP851] [GN:RP851] [OR:Rickettsiaprowazekii] 93 SPX1026 1026 3687 84 252 139 1.80E-13 [LN:F72338][AC:F72338] [PN:conserved hypothetical protein] [GN:TM0731][OR:Thermotoga maritima] 96 SPX1027 1027 3688 64 192 NO-HIT 6 SPX10281028 3689 258 774 129 6.70E-09 [LN:T33885] [AC:T33885] [PN:hypotheticalprotein H14E04.1] [GN:H14E04.1] [CL:24-sterol C-methyltransferase:bioChomology] [OR:Caenorhabditis elegans] 149 SPX1029 1029 3690 113 339 1331.50E-11 [LN:AB025228] [AC:AB025228] [GN:rgg] [OR:Streptococcus oralis][SR:Streptococcus oralis (strain:ATCC10557) DNA] 111 SPX1030 1030 3691116 348 90 8.90E-06 [LN:AB025228] [AC:AB025228] [GN:rgg][OR:Streptococcus oralis] [SR:Streptococcus oralis (strain:ATCC10557)DNA] 111 SPX1031 1031 3692 178 534 294 4.90E-36 [LN:F69815] [AC:F69815][PN:hypothetical protein ygaC] [GN:ygaC] [CL:Bacillus subtilishypothetical protein ygaC] [OR:Bacillus subtilis] 136 SPX1032 1032 369360 180 NO-HIT 6 SPX1033 1033 3694 287 861 226 3.30E-32 [LN:H69800][AC:H69800] [PN:hypothetical protein yfhG] [GN:yfhG] [OR:Bacillussubtilis] 87 SPX1034 1034 3695 452 1356 606 1.00E-145 [LN:F69806][AC:F69806] [PN:RNA methyltransferase homolog yfjO] [GN:yfjO][CL:hypothetical protein HI0333] [OR:Bacillus subtilis] 129 SPX1035 10353696 82 246 NO-HIT 6 SPX1036 1036 3697 50 150 82 7.60E-06 [LN:G71244][AC:G71244] [PN:hypothetical protein PH0217] [GN:PH0217] [OR:Pyrococcushorikoshii] 95 SPX1037 1037 3698 62 186 NO-HIT 6 SPX1038 1038 3699 87261 136 3.90E-14 [LN:G81516] [AC:G81516] [PN:hypothetical protein CP0988[imported]] [GN:CP0988] [OR:Chlamydophila pneumoniae:Chlamydiapneumoniae] 130 SPX1039 1039 3700 76 228 190 1.00E-21 [LN:T30285][AC:T30285] [PN:hypothetical protein] [OR:Streptococcus pneumoniae] 79SPX1040 1040 3701 79 237 NO-HIT 6 SPX1041 1041 3702 94 282 301 2.00E-35[LN:DHAS_STRMU] [AC:P10539] [GN:ASD] [OR:Streptococcus mutans][EC:1.2.1.11] [DE:DEHYDROGENASE)] [SP:P10539] 108 SPX1042 1042 3703 92276 325 3.80E-40 [LN:DHAS_STRMU] [AC:P10539] [GN:ASD] [OR:Streptococcusmutans] [EC:1.2.1.11] [DE:DEHYDROGENASE)] [SP:P10539] 108 SPX1043 10433704 222 666 590 1.20E-108 [LN:DHAS_STRMU] [AC:P10539] [GN:ASD][OR:Streptococcus mutans] [EC:1.2.1.11] [DE:DEHYDROGENASE)] [SP:P10539]108 SPX1044 1044 3705 312 936 192 2.60E-55 [LN:B72246] [AC:B72246][PN:dihydrodipicolinate synthase, TM1521 [similarity]] [GN:TM1521][CL:Pseudomonas 5-dehydro-4-deoxyglucarate dehydratase] [OR:Thermotogamaritima] [EC:4.2.1.52] 187 SPX1045 1045 3706 458 1374 1312 1.10E-249[GI:6448626] [LN:SAG251564] [AC:AJ251564] [PN:thiophene degradationprotein F] [GN:thdF] [FN:putative thiophene and furan oxidation gene][OR:Streptococcus agalactiae] 167 SPX1046 1046 3707 75 225 127 1.30E-12[LN:A43397] [AC:A43397:S35225] [PN:4-oxalocrotonate tautomerase, xylH][GN:xylH] [CL:4-oxalocrotonate tautomerase] [OR:Pseudomonas putida][EC:5.3.2.-] 153 SPX1047 1047 3708 164 492 724 7.00E-97 [LN:KITH_STRGC][AC:P47848] [GN:TDK] [OR:Streptococcus gordonii challis] [EC:2.7.1.21][DE:THYMIDINE KINASE,] [SP:P47848] 123 SPX1048 1048 3709 281 843 6422.20E-103 [LN:RF1_BACSU] [AC:P45872] [GN:PRFA] [OR:Bacillus subtilis][DE:PEPTIDE CHAIN RELEASE FACTOR 1 (RF-1)] [SP:P45872] 114 SPX1049 10493710 143 429 350 2.60E-43 [LN:RF1_BACSU] [AC:P45872] [GN:PRFA][OR:Bacillus subtilis] [DE:PEPTIDE CHAIN RELEASE FACTOR 1 (RF-1)][SP:P45872] 114 SPX1050 1050 3711 280 840 183 8.00E-41 [LN:HEMK_BACSU][AC:P45873] [GN:YWKE] [OR:Bacillus subtilis] [DE:HEMK PROTEIN HOMOLOG][SP:P45873] 98 SPX1051 1051 3712 201 603 244 1.80E-32 [GI:6015811][LN:SSU18930] [AC:Y18930] [PN:hypothetical protein] [GN:ORF-c09_003][OR:Sulfolobus solfataricus] 110 SPX1052 1052 3713 144 432 97 1.30E-05[LN:PHNO_ECOLI] [AC:P16691] [GN:PHNO] [OR:Escherichia coli] [DE:PHNOPROTEIN] [SP:P16691] 89 SPX1053 1053 3714 419 1257 858 7.90E-176[LN:GLYA_BACSU] [AC:P39148] [GN:GLYA:GLYC:IPC-34D] [OR:Bacillussubtilis] [EC:2.1.2.1] [DE:(SHMT)] [SP:P39148] 110 SPX1054 1054 3715 3361008 130 3.90E-11 [GI:6899993] [LN:CST130879] [AC:AJ130879][PN:hypothetical protein] [FN:unknown] [OR:Clostridium sticklandii] 109SPX1055 1055 3716 205 615 243 1.60E-27 [LN:F69900] [AC:F69900][PN:transposon-related protein homolog yocA] [GN:yocA] [OR:Bacillussubtilis] 101 SPX1056 1056 3717 325 975 104 7.60E-08 [LN:YPUA_BACSU][AC:P31847:P37951] [GN:YPUA] [OR:Bacillus subtilis] [DE:HYPOTHETICAL31.3 KD PROTEIN IN LYSA-PPIB INTERGENIC REGION (ORFX19)][SP:P31847:P37951] 160 SPX1057 1057 3718 548 1644 767 5.90E-131[LN:E69793] [AC:E69793] [PN:RNA methyltransferase homolog yefA][GN:yefA] [CL:hypothetical protein HI0333] [OR:Bacillus subtilis] 129SPX1058 1058 3719 98 294 NO-HIT 6 SPX1059 1059 3720 83 249 NO-HIT 6SPX1060 1060 3721 65 195 81 3.20E-08 [LN:C69931] [AC:C69931][PN:transcription regulator homolog yozG] [GN:yozG] [OR:Bacillussubtilis] 98 SPX1061 1061 3722 80 240 NO-HIT 6 SPX1062 1062 3723 3451035 276 3.80E-70 [GI:2276374] [LN:CDU02617] [AC:U02617] [PN:DtxR/ironregulated lipoprotein precursor] [GN:irp1] [FN:iron transport][OR:Corynebacterium diphtheriae] 148 SPX1063 1063 3724 212 636 NO-HIT 6SPX1064 1064 3725 336 1008 643 1.40E-86 [LN:T44797] [AC:T44797] [PN:irontransport membrane protein irp1B [imported]] [GN:irp1B] [CL:vitamin B12transport protein btuC] [OR:Corynebacterium diphtheriae] 161 SPX10651065 3726 336 1008 484 1.10E-82 [LN:T44798] [AC:T44798] [PN:irontransport membrane protein irp1C [imported]] [GN:irp1C] [CL:vitamin B12transport protein btuC] [OR:Corynebacterium diphtheriae] 161 SPX10661066 3727 74 222 NO-HIT 6 SPX1067 1067 3728 138 414 NO-HIT 6 SPX10681068 3729 265 795 694 6.10E-91 [LN:G70022] [AC:G70022] [PN:iron(III)dicitrate transport permease homolog yusV] [GN:yusV] [CL:inner membraneprotein malK:ATP-binding cassette homology] [OR:Bacillus subtilis] 176SPX1069 1069 3730 87 261 151 1.30E-14 [GI:2467226] [LN:LLLPK214][AC:X92946:Y10522] [PN:transposase] [GN:tnpA] [OR:Lactococcus lactis] 96SPX1070 1070 3731 152 456 137 1.10E-10 [LN:T4BB_BACCO] [AC:Q07606][GN:BCGIB] [OR:Bacillus coagulans] [EC:3.1.21.-] [DE:RESTRICTION ENZYMEBGCI BETA SUBUNIT,] [SP:Q07606] 133 SPX1071 1071 3732 92 276 NO-HIT 6SPX1072 1072 3733 83 249 NO-HIT 6 SPX1073 1073 3734 70 210 NO-HIT 6SPX1074 1074 3735 560 1680 138 3.40E-35 [GI:6681569] [LN:AB014436][AC:AB014436] [PN:cassette chromosome recombinase B] [GN:ccrB][OR:Staphylococcus aureus] [SR:Staphylococcus aureus (strain:85/2082)DNA] 164 SPX1075 1075 3736 204 612 NO-HIT 6 SPX1076 1076 3737 63 189NO-HIT 6 SPX1077 1077 3738 253 759 NO-HIT 6 SPX1078 1078 3739 285 855 704.40E-09 [GI:7020551] [LN:AK000453] [AC:AK000453] [OR:Homo sapiens][SR:Homo sapiens signet-ring cell carcinoma cell_line:KATO III cDNA t]129 SPX1079 1079 3740 295 885 192 4.90E-36 [LN:F69795] [AC:F69795][PN:conserved hypothetical protein yerQ] [GN:yerQ] [OR:Bacillussubtilis] 97 SPX1080 1080 3741 93 279 124 1.30E-19 [LN:JS0673][AC:JS0673] [PN:neopullulanase,] [CL:neopullulanase:alpha-amylase corehomology] [OR:Bacillus sp.] [EC:3.2.1.135] 127 SPX1081 1081 3742 4851455 683 3.10E-176 [LN:F70033] [AC:F70033] [PN:glucan1,4-alpha-maltohydrolase homolog yvdF] [GN:yvdF][CL:neopullulanase:alpha-amylase core homology] [OR:Bacillus subtilis]156 SPX1082 1082 3743 101 303 NO-HIT 6 SPX1083 1083 3744 143 429 2499.00E-30 [GI:6102604] [LN:AF144880] [AC:AF144880] [PN:aminoglycoside6′-N-acetyltransferase] [GN:aac(6′)-Iy] [OR:Salmonella enteritidis] 127SPX1084 1084 3745 190 570 NO-HIT 6 SPX1085 1085 3746 71 213 NO-HIT 6SPX1086 1086 3747 94 282 NO-HIT 6 SPX1087 1087 3748 65 195 184 8.80E-20[LN:S52544] [AC:S52544] [PN:ISL2 protein] [OR:Lactobacillus helveticus]71 SPX1088 1088 3749 410 1230 419 1.50E-74 [LN:FTSW_ENTHR] [AC:Q47866][GN:FTSW] [OR:Enterococcus hirae] [DE:PROBABLE CELL DIVISION PROTEINFTSW] [SP:Q47866] 114 SPX1089 1089 3750 899 2697 418 1.60E-169[GI:144985] [LN:CORPEPC] [AC:M25819] [PN:phosphoenolpyruvatecarboxylase] [OR:Corynebacterium glutamicum] [SR:Corynebacteriumglutamicum (clone: pTG1200.) (tissue library: ATC] 176 SPX1090 1090 3751102 306 NO-HIT 6 SPX1091 1091 3752 210 630 105 2.60E-05 [LN:H71693][AC:H71693] [PN:hypothetical protein RP367] [GN:RP367] [OR:Rickettsiaprowazekii] 93 SPX1092 1092 3753 223 669 163 6.00E-23 [LN:A71694][AC:A71694] [PN:hypothetical protein RP368] [GN:RP368] [OR:Rickettsiaprowazekii] 93 SPX1093 1093 3754 253 759 365 1.80E-45 [GI:1661179][LN:SMU75471] [AC:U75471] [PN:high affinity branched chain amino acid][GN:livG] [OR:Streptococcus mutans] 119 SPX1094 1094 3755 64 192 822.10E-05 [LN:A71007] [AC:A71007] [PN:hypothetical protein PH1351][GN:PH1351] [OR:Pyrococcus horikoshii] 95 SPX1095 1095 3756 592 1776 6941.40E-161 [LN:PRIM_LACLA] [AC:Q04505] [GN:DNAG:DNAE] [OR:Lactococcuslactis] [SR:,subsplactis:Streptococcus lactis] [EC:2.7.7.-] [DE:DNAPRIMASE,] [SP:Q04505] 150 SPX1096 1096 3757 305 915 1452 2.30E-194[LN:RPOD_STRPN] [AC:O08388] [GN:RPOD] [OR:Streptococcus pneumoniae][DE:RNA POLYMERASE SIGMA FACTOR RPOD] [SP:O08388] 117 SPX1097 1097 375866 198 290 2.40E-35 [LN:RPOD_STRPN] [AC:O08388] [GN:RPOD][OR:Streptococcus pneumoniae] [DE:RNA POLYMERASE SIGMA FACTOR RPOD][SP:O08388] 117 SPX1098 1098 3759 110 330 556 5.10E-73 [GI:2108332][LN:SPDNAGCPO] [AC:Y11463] [OR:Streptococcus pneumoniae] 69 SPX1099 10993760 69 207 NO-HIT 6 SPX1100 1100 3761 267 801 1357 1.40E-186[GI:2108333] [LN:SPDNAGCPO] [AC:Y11463] [GN:cpoA] [OR:Streptococcuspneumoniae] 79 SPX1101 1101 3762 66 198 318 4.00E-38 [GI:2108333][LN:SPDNAGCPO] [AC:Y11463] [GN:cpoA] [OR:Streptococcus pneumoniae] 79SPX1102 1102 3763 442 1326 1475 1.70E-200 [GI:2108334] [LN:SPDNAGCPO][AC:Y11463] [OR:Streptococcus pneumoniae] 69 SPX1103 1103 3764 59 177151 3.70E-16 [LN:B72287] [AC:B72287] [PN:conserved hypothetical protein][GN:TM1156] [OR:Thermotoga maritima] 96 SPX1104 1104 3765 392 1176 10215.10E-184 [LN:OBG_BACSU] [AC:P20964] [GN:OBG] [OR:Bacillus subtilis][DE:SPO0B-ASSOCIATED GTP-BINDING PROTEIN] [SP:P20964] 112 SPX1105 11053766 420 1260 424 9.00E-142 [LN:MURA_BACSU] [AC:P19670:Q03225][GN:MURA:MURZ] [OR:Bacillus subtilis] [EC:2.5.1.7] [DE:ENOLPYRUVYLTRANSFERASE) (EPT)] [SP:P19670:Q03225] 140 SPX1106 1106 3767 176 528 1561.00E-17 [LN:C69895] [AC:C69895] [PN:conserved hypothetical proteinyoaA] [GN:yoaA] [CL:Escherichia coli ribosomal-protein-alanineN-acetyltransferase rimJ] [OR:Bacillus subtilis] 170 SPX1107 1107 3768426 1278 425 4.20E-85 [LN:A69998] [AC:A69998] [PN:hypothetical proteinytoI] [GN:ytoI] [OR:Bacillus subtilis] 87 SPX1108 1108 3769 287 861 3453.30E-65 [LN:T44405] [AC:T44405] [PN:methionyl aminopeptidase, map[imported]] [CL:Escherichia coli methionyl aminopeptidase] [OR:Bacillushalodurans] [EC:3.4.11.18] 158 SPX1109 1109 3770 181 543 307 2.50E-38[LN:S52544] [AC:S52544] [PN:ISL2 protein] [OR:Lactobacillus helveticus]71 SPX1110 1110 3771 75 225 104 5.80E-08 [LN:S52544] [AC:S52544][PN:ISL2 protein] [OR:Lactobacillus helveticus] 71 SPX1111 1111 3772 130390 384 4.80E-49 [LN:S52544] [AC:S52544] [PN:ISL2 protein][OR:Lactobacillus helveticus] 71 SPX1112 1112 3773 764 2292 13517.70E-282 [LN:E69794] [AC:E69794] [PN:ATP-dependent DNA helicase homologyerF] [GN:yerF] [CL:helicase II] [OR:Bacillus subtilis] 118 SPX1113 11133774 240 720 488 2.80E-62 [LN:RADC_BACSU] [AC:Q02170] [GN:YSXA][OR:Bacillus subtilis] [DE:DNA REPAIR PROTEIN RADC HOMOLOG (ORFB)][SP:Q02170] 116 SPX1114 1114 3775 230 690 237 6.50E-27 [LN:YDP3_LACLA][AC:P22347] [OR:Lactococcus lactis] [SR:,subsplactis:Streptococcuslactis] [DE:HYPOTHETICAL 18.7 KD PROTEIN IN PEPX 3′REGION (ORF3)][SP:P22347] 162 SPX1115 1115 3776 214 642 339 2.60E-68 [LN:A69787][AC:A69787] [PN:hypothetical protein ydiH] [GN:ydiH] [OR:Bacillussubtilis] 87 SPX1116 1116 3777 84 252 NO-HIT 6 SPX1117 1117 3778 116 348NO-HIT 6 SPX1118 1118 3779 265 795 288 2.40E-63 [LN:E69981] [AC:E69981][PN:iron-sulfur cofactor synthesis protein yrvO] [GN:yrvO] [CL:nitrogenfixation protein nifS] [OR:Bacillus subtilis] 141 SPX1119 1119 3780 145435 149 4.90E-18 [GI:2289093] [LN:CAU76387] [AC:U76387] [PN:PRPPsynthetase] [GN:prs] [OR:Corynebacterium ammoniagenes] 102 SPX1120 11203781 183 549 547 6.60E-75 [GI:2289093] [LN:CAU76387] [AC:U76387][PN:PRPP synthetase] [GN:prs] [OR:Corynebacterium ammoniagenes] 102SPX1121 1121 3782 190 570 164 1.20E-26 [LN:C69844] [AC:C69844][PN:hypothetical protein yjbK] [GN:yjbK] [CL:Bacillus subtilishypothetical protein yjbK] [OR:Bacillus subtilis] 136 SPX1122 1122 3783168 504 338 6.80E-68 [LN:E69844] [AC:E69844] [PN:GTP pyrophosphokinasehomolog yjbM] [GN:yjbM] [CL:GTP pyrophosphokinase related protein][OR:Bacillus subtilis] 139 SPX1123 1123 3784 71 213 90 6.20E-06[LN:E69844] [AC:E69844] [PN:GTP pyrophosphokinase homolog yjbM][GN:yjbM] [CL:GTP pyrophosphokinase related protein] [OR:Bacillussubtilis] 139 SPX1124 1124 3785 263 789 309 4.70E-67 [LN:F69844][AC:F69844] [PN:conserved hypothetical protein yjbN] [GN:yjbN][CL:conserved hypothetical protein HI0072] [OR:Bacillus subtilis] 140SPX1125 1125 3786 299 897 286 3.40E-66 [LN:YJBO_BACSU] [AC:O31613][GN:YJBO] [OR:Bacillus subtilis] [DE:HYPOTHETICAL 31.5 KD PROTEIN INMECA-TENA INTERGENIC REGION] [SP:O31613] 137 SPX1126 1126 3787 325 975867 5.10E-115 [LN:PTA_BACSU] [AC:P39646] [GN:PTA:IPA-88D] [OR:Bacillussubtilis] [EC:2.3.1.8] [DE:(PHOSPHOTRANSACETYLASE) (VEGETATIVE PROTEIN43) (VEG43)] [SP:P39646] 152 SPX1127 1127 3788 79 237 NO-HIT 6 SPX11281128 3789 199 597 472 3.10E-122 [GI:663279] [LN:STRCOMAA][AC:M36180:L15190] [PN:transposase] [OR:Streptococcus pneumoniae][SR:Streptococcus pneumoniae (strain RX1) DNA] 138 SPX1129 1129 3790 109327 280 2.00E-34 [GI:2804700] [LN:AF030361] [AC:AF030361][PN:transposase] [OR:Streptococcus pneumoniae] 87 SPX1130 1130 3791 173519 875 3.10E-119 [GI:663278] [LN:STRCOMAA] [AC:M36180:L15190][PN:transposase] [OR:Streptococcus pneumoniae] [SR:Streptococcuspneumoniae (strain RX1) DNA] 138 SPX1131 1131 3792 108 324 190 3.90E-21[LN:YAAK_BACSU] [AC:P24281] [GN:YAAK] [OR:Bacillus subtilis][DE:HYPOTHETICAL 11.8 KD PROTEIN IN DNAZ-RECR INTERGENIC REGION][SP:P24281] 137 SPX1132 1132 3793 231 693 89 1.90E-05 [LN:E69896][AC:E69896] [PN:hypothetical protein yoaK] [GN:yoaK] [OR:Bacillussubtilis] 87 SPX1133 1133 3794 105 315 360 3.20E-44 [LN:RL21_BACSU][AC:P26908] [GN:RPLU] [OR:Bacillus subtilis] [DE:50S RIBOSOMAL PROTEINL21 (BL20)] [SP:P26908] 110 SPX1134 1134 3795 147 441 NO-HIT 6 SPX11351135 3796 115 345 152 1.30E-22 [LN:YSXB_BACSU] [AC:P26942:Q45629][GN:YSXB] [OR:Bacillus subtilis] [DE:HYPOTHETICAL 12.3 KD PROTEIN INRPLU-RPMA INTERGENIC REGION (ORF X)] [SP:P26942:Q45629] 159 SPX1136 11363797 98 294 372 1.10E-46 [LN:RL27_BACSU] [AC:P05657] [GN:RPMA][OR:Bacillus subtilis] [DE:50S RIBOSOMAL PROTEIN L27 (BL30) (BL24)][SP:P05657] 117 SPX1137 1137 3798 55 165 77 4.70E-09 [GI:1914870][LN:SPZ82001] [AC:Z82001] [PN:unknown] [OR:Streptococcus pneumoniae] 81SPX1138 1138 3799 306 918 808 1.30E-107 [GI:2289231] [LN:SAU92073][AC:U92073] [PN:macrolide-efflux protein] [GN:mreA] [FN:resistance to14- and 15-membered macrolides] [OR:Streptococcus agalactiae] 158SPX1139 1139 3800 283 849 531 2.80E-71 [LN:YPJC_BACSU] [AC:P42978][GN:YPJC:JOJC] [OR:Bacillus subtilis] [DE:HYPOTHETICAL 23.6 KD PROTEININ QCRC-DAPB INTERGENIC REGION] [SP:P42978] 142 SPX1140 1140 3801 280840 252 9.50E-36 [GI:671632] [LN:SADIRED] [AC:Z16422] [PN:unknown][GN:ORF2] [OR:Staphylococcus aureus] 86 SPX1141 1141 3802 92 276 3979.60E-50 [GI:5209334] [LN:L40356] [AC:L40356] [PN:histone-likeDNA-binding protein] [GN:hlpA] [OR:Streptococcus gordonii] 112 SPX11421142 3803 634 1902 905 2.00E-202 [LN:YDIF_BACSU] [AC:O05519] [GN:YDIF][OR:Bacillus subtilis] [DE:HYPOTHETICAL ABC TRANSPORTER ATP-BINDINGPROTEIN YDIF] [SP:O05519] 131 SPX1143 1143 3804 298 894 204 8.40E-33[GI:4102023] [LN:AF007761] [AC:AF007761] [PN:MutR] [GN:mutR][FN:positive transcriptional regulator of mutA] [OR:Streptococcusmutans] 134 SPX1144 1144 3805 393 1179 113 5.30E-22 [LN:H72265][AC:H72265] [PN:hypothetical protein TM1336] [GN:TM1336] [OR:Thermotogamaritima] 93 SPX1145 1145 3806 656 1968 521 1.40E-217 [LN:F69794][AC:F69794] [PN:DNA ligase (NAD+),] [GN:yerG][CL:polydeoxyribonucleotide synthase (NAD+)] [OR:Bacillus subtilis][EC:6.5.1.2] 140 SPX1146 1146 3807 760 2280 620 2.20E-109 [GI:3089609][LN:AF060205] [AC:AF060205] [PN:pullulanase] [GN:pul] [OR:Thermus sp.IM6501] 90 SPX1147 1147 3808 475 1425 1818 2.70E-245 [LN:GAPN_STRMU][AC:Q59931] [GN:GAPN] [OR:Streptococcus mutans] [EC:1.2.1.9][DE:DEHYDROGENASE)] [SP:Q59931] 108 SPX1148 1148 3809 643 1929 6586.60E-176 [LN:S18599] [AC:S18599] [PN:1,4-alpha-glucan branchingenzyme,:glycogen branching enzyme] [CL:1,4-alpha-glucan branchingenzyme] [OR:Bacillus stearothermophilus] [EC:2.4.1.18] 177 SPX1149 11493810 381 1143 187 6.00E-19 [LN:CCE277601] [AC:AJ277601] [PN:ADP-glucosepyrophosphorylase] [GN:glgD] [OR:Clostridium cellulolyticum] 105 SPX11501150 3811 380 1140 324 4.80E-53 [LN:GLGD_BACST] [AC:O08327] [GN:GLGD][OR:Bacillus stearothermophilus] [DE:GLYCOGEN BIOSYNTHESIS PROTEIN GLGD][SP:O08327] 122 SPX1151 1151 3812 478 1434 813 6.80E-159 [LN:GLGA_BACSU][AC:P39125] [GN:GLGA] [OR:Bacillus subtilis] [EC:2.4.1.21][DE:SYNTHASE)] [SP:P39125] 101 SPX1152 1152 3813 124 372 214 7.80E-24[LN:B69517] [AC:B69517] [PN:phosphoserine phosphatase (serB) homolog][OR:Archaeoglobus fulgidus] 97 SPX1153 1153 3814 110 330 213 6.30E-24[LN:A64499] [AC:A64499] [PN:phosphoserine phosphatase,][CL:phosphoserine phosphatase] [OR:Methanococcus jannaschii][EC:3.1.3.3] 131 SPX1154 1154 3815 372 1116 1670 1.30E-226 [GI:7380122][LN:NMA5Z2491] [AC:AL162756:AL157959] [PN:hypothetical protein NMA1473][GN:NMA1473] [OR:Neisseria meningitidis] 125 SPX1155 1155 3816 149 447NO-HIT 6 SPX1156 1156 3817 435 1305 2119 6.30E-286 [GI:5263171][LN:AB029313] [AC:AB029313] [PN:enolase] [GN:eno] [OR:Streptococcusintermedius] [SR:Streptococcus intermedius (strain:ATCC 27335) DNA] 148SPX1157 1157 3818 156 468 74 6.80E-09 [LN:T45116] [AC:T45116][PN:phosphopyruvate hydratase, [imported]] [OR:Schizosaccharomycespombe] [EC:4.2.1.11] 113 SPX1158 1158 3819 44 132 75 2.00E-06[LN:B72477] [AC:B72477] [PN:hypothetical protein APE2459] [GN:APE2459][OR:Aeropyrum pernix] 92 SPX1159 1159 3820 169 507 174 3.60E-16[GI:6782411] [LN:STH243106] [AC:AJ243106] [PN:integrase] [GN:int][OR:Streptococcus thermophilus] 97 SPX1160 1160 3821 113 339 5566.20E-74 [GI:5019553] [LN:SPN239004] [AC:AJ239004] [PN:putativetransposase] [OR:Streptococcus pneumoniae] 97 SPX1161 1161 3822 116 348573 1.80E-75 [GI:4200438] [LN:AF026471] [AC:AF026471] [PN:putativetransposase] [OR:Streptococcus pneumoniae] 96 SPX1162 1162 3823 10923276 315 2.90E-101 [LN:T30307] [AC:T30307] [PN:rexB protein] [GN:rexB][OR:Lactococcus lactis] 75 SPX1163 1163 3824 1217 3651 517 1.80E-246[LN:T30308] [AC:T30308] [PN:rexA protein] [OR:Lactococcus lactis] 65SPX1164 1164 3825 79 237 NO-HIT 6 SPX1165 1165 3826 64 192 205 2.00E-24[LN:T30285] [AC:T30285] [PN:hypothetical protein] [OR:Streptococcuspneumoniae] 79 SPX1166 1166 3827 393 1179 NO-HIT 6 SPX1167 1167 3828 111333 NO-HIT 6 SPX1168 1168 3829 1966 5898 7485 0 [GI:1213494][LN:SPU47687] [AC:U47687] [PN:immunoglobulin A1 protease] [GN:iga][OR:Streptococcus pneumoniae] [SR:Streptococcus pneumoniae strain=R6]149 SPX1169 1169 3830 76 228 138 8.00E-12 [GI:6911257] [LN:AF221126][AC:AF221126] [PN:putative zinc metalloprotease] [GN:zmpB][OR:Streptococcus pneumoniae] 115 SPX1170 1170 3831 284 852 707 2.50E-96[LN:F69880] [AC:F69880] [PN:conserved hypothetical protein ylqF][GN:ylqF] [CL:conserved hypothetical protein MG442] [OR:Bacillussubtilis] 139 SPX1171 1171 3832 260 780 615 3.40E-79 [LN:C69693][AC:C69693] [PN:ribonuclease H rnh] [GN:rnh] [CL:ribonuclease HII][OR:Bacillus subtilis] 101 SPX1172 1172 3833 517 1551 261 1.40E-51[LN:YADQ_ECOLI] [AC:P37019:P77394] [GN:YADQ] [OR:Escherichia coli][DE:HYPOTHETICAL 46.0 KD PROTEIN IN HEML-PFS INTERGENIC REGION][SP:P37019:P77394] 149 SPX1173 1173 3834 357 1071 1529 9.60E-206[GI:3152920] [LN:AF065141] [AC:AF065141] [PN:unknown] [OR:Streptococcusmutans] 79 SPX1174 1174 3835 330 990 577 6.60E-108 [LN:G69830][AC:G69830] [PN:lipoate-protein ligase homolog yhfJ] [GN:yhfJ][CL:lipoate-protein ligase] [OR:Bacillus subtilis] 125 SPX1175 1175 3836568 1704 334 6.80E-104 [LN:I40794] [AC:I40794] [PN:dihydrolipoamidedehydrogenase] [OR:Clostridium magnum] [EC:1.8.1.4] 96 SPX1176 1176 3837376 1128 366 8.20E-70 [LN:I40793] [AC:I40793] [PN:dihydrolipoamideS-acetyltransferase,] [CL:dihydrolipoamideacetyltransferase:lipoyl/biotin-binding homology] [OR:Clostridiummagnum] [EC:2.3.1.12] 177 SPX1177 1177 3838 331 993 550 5.00E-108[LN:I40791] [AC:I40791] [PN:acetoin dehydrogenase (TPP-dependent), betachain] [CL:pyruvate dehydrogenase (lipoamide) beta chain][OR:Clostridium magnum] [EC:1.-.-.-] 168 SPX1178 1178 3839 146 438NO-HIT 6 SPX1179 1179 3840 104 312 136 6.90E-13 [LN:G72548] [AC:G72548][PN:hypothetical protein APE1675] [GN:APE1675] [OR:Aeropyrum pernix] 92SPX1180 1180 3841 323 969 554 6.20E-107 [LN:I40790] [AC:I40790][PN:acetoin dehydrogenase (TPP-dependent), alpha chain] [CL:pyruvatedehydrogenase (lipoamide) alpha chain:thiamin pyrophosphate-bindingdomain homology] [OR:Clostridium magnum] [EC:1.-.-.-] 216 SPX1181 11813842 454 1362 482 2.40E-117 [LN:F69906] [AC:F69906] [PN:conservedhypothetical protein yojI] [GN:yojI] [CL:conserved hypothetical proteinHI1612] [OR:Bacillus subtilis] 140 SPX1182 1182 3843 87 261 NO-HIT 6SPX1183 1183 3844 423 1269 351 1.70E-86 [LN:PYRC_LACLE] [AC:P48795][GN:PYRC] [OR:Lactobacillus leichmannii] [EC:3.5.2.3][DE:DIHYDROOROTASE, (DHOASE)] [SP:P48795] 125 SPX1184 1184 3845 155 465845 7.70E-113 [LN:MUTX_STRPN] [AC:P41354] [GN:MUTX] [OR:Streptococcuspneumoniae] [EC:3.6.1.-] [DE:(8-OXO-DGTPASE), (DGTPPYROPHOSPHOHYDROLASE)] [SP:P41354] 144 SPX1185 1185 3846 222 666 11238.50E-151 [LN:UNG_STRPN] [AC:P23379] [GN:UNG] [OR:Streptococcuspneumoniae] [EC:3.2.2.-] [DE:URACIL-DNA GLYCOSYLASE, (UDG)] [SP:P23379]127 SPX1186 1186 3847 201 603 NO-HIT 6 SPX1187 1187 3848 238 714 2605.40E-57 [LN:E69814] [AC:E69814] [PN:conserved hypothetical proteinyfnB] [GN:yfnB] [CL:Alcaligenes eutrophus phosphoglycolate phosphatase][OR:Bacillus subtilis] 153 SPX1188 1188 3849 76 228 66 1.60E-05[LN:H75623] [AC:H75623] [PN:conserved hypothetical protein] [GN:DRB0052][OR:Deinococcus radiodurans] 101 SPX1189 1189 3850 852 2556 4123.10E-104 [LN:T46758] [AC:T46758] [PN:hypothetical protein [imported]][OR:Streptococcus agalactiae] 90 SPX1190 1190 3851 830 2490 3973.60E-100 [LN:T46758] [AC:T46758] [PN:hypothetical protein [imported]][OR:Streptococcus agalactiae] 90 SPX1191 1191 3852 411 1233 17634.80E-237 [GI:4958916] [LN:AB027569] [AC:AB027569][PN:phosphoenolpyruvate-protein phosphotransferase] [GN:ptsI][OR:Streptococcus bovis] [SR:Streptococcus bovis (strain:JB1) DNA] 169SPX1192 1192 3853 46 138 144 1.50E-15 [LN:YKXH_BACSU] [AC:P08876][GN:YKXH] [OR:Bacillus subtilis] [DE:HYPOTHETICAL 7.4 KD PROTEIN IN PTSXOPERON (PROTEIN K)] [SP:P08876] 132 SPX1193 1193 3854 88 264 4022.30E-50 [LN:PTHP_STRMU] [AC:P45596] [GN:PTSH] [OR:Streptococcus mutans][DE:PHOSPHOCARRIER PROTEIN HPR (HISTIDINE-CONTAINING PROTEIN)][SP:P45596] 138 SPX1194 1194 3855 73 219 233 1.50E-27 [LN:NRDH_LACLC][AC:Q48708] [GN:NRDH] [OR:Lactococcus lactis][SR:,subspcremoris:Streptococcus cremoris] [DE:GLUTAREDOXIN-LIKE PROTEINNRDH] [SP:Q48708] 154 SPX1195 1195 3856 720 2160 1042 2.20E-255[GI:3077613] [LN:CANRDFGEN] [AC:Y09572] [PN:ribonucleotide reductasesubunit R1E] [GN:nrdE] [OR:Corynebacterium ammoniagenes] 125 SPX11961196 3857 63 189 NO-HIT 6 SPX1197 1197 3858 321 963 818 2.90E-116[GI:3068719] [LN:AF050168] [AC:AF050168] [PN:ribonucleoside diphosphatereductase small] [GN:nrdF] [OR:Corynebacterium ammoniagenes] 132 SPX11981198 3859 254 762 371 2.50E-80 [LN:LACR_LACLA] [AC:P18816] [GN:LACR][OR:Lactococcus lactis] [SR:,subsplactis:Streptococcus lactis][DE:LACTOSE PHOSPHOTRANSFERASE SYSTEM REPRESSOR] [SP:P18816] 163 SPX11991199 3860 84 252 NO-HIT 6 SPX1200 1200 3861 472 1416 2452 0[LN:LACG_LACLA] [AC:P11546] [GN:LACG] [OR:Lactococcus lactis][SR:,subsplactis:Streptococcus lactis] [EC:3.2.1.85][DE:GALACTOHYDROLASE) (PGALASE) (P-BETA-GAL) (PBG)] [SP:P11546] 180SPX1201 1201 3862 565 1695 1628 4.50E-299 [LN:PTLB_LACLA] [AC:P23531][GN:LACE] [OR:Lactococcus lactis] [SR:,subsplactis:Streptococcus lactis][EC:2.7.1.69] [DE:(EC 2.7.1.69) (EII-LAC)] [SP:P23531] 157 SPX1202 12023863 106 318 454 2.90E-58 [LN:PTLA_LACLA] [AC:P23532] [GN:LACF][OR:Lactococcus lactis] [SR:,subsplactis:Streptococcus lactis][EC:2.7.1.69] [DE:(EC 2.7.1.69) (EIII-LAC)] [SP:P23532] 158 SPX1203 12033864 279 837 487 1.40E-75 [LN:LACT_LACCA] [AC:P24401] [GN:LACT][OR:Lactobacillus casei] [DE:TRANSCRIPTION ANTITERMINATOR LACT][SP:P24401] 113 SPX1204 1204 3865 270 810 1232 1.10E-164 [LN:LACD_LACLA][AC:P26593] [GN:LACD] [OR:Lactococcus lactis][SR:,subsplactis:Streptococcus lactis] [EC:4.1.2.40] [DE:ALDOLASE)(D-TAGATOSE-1,6-BISPHOSPHATE ALDOLASE)] [SP:P26593] 182 SPX1205 12053866 273 819 810 9.10E-118 [LN:LACC_LACLA] [AC:P23391] [GN:LACC][OR:Lactococcus lactis] [SR:,subsplactis:Streptococcus lactis][EC:2.7.1.144] [DE:TAGATOSE-6-PHOSPHATE KINASE, (PHOSPHOTAGATOKINASE)][SP:P23391] 185 SPX1206 1206 3867 163 489 NO-HIT 6 SPX1207 1207 3868 172516 810 5.00E-108 [LN:LACB_LACLA] [AC:P23495] [GN:LACB] [OR:Lactococcuslactis] [SR:,subsplactis:Streptococcus lactis] [EC:5.3.1.26][DE:GALACTOSE-6-PHOSPHATE ISOMERASE LACB SUBUNIT,] [SP:P23495] 179SPX1208 1208 3869 142 426 612 2.90E-80 [LN:LACA_LACLA] [AC:P23494][GN:LACA] [OR:Lactococcus lactis] [SR:,subsplactis:Streptococcus lactis][EC:5.3.1.26] [DE:GALACTOSE-6-PHOSPHATE ISOMERASE LACA SUBUNIT,][SP:P23494] 179 SPX1209 1209 3870 97 291 57 0.00024 [GI:712785][LN:S74218] [AC:S74218] [GN:E9] [OR:reindeer papillomavirus] 72 SPX12101210 3871 159 477 507 1.70E-65 [LN:LAXP_LACLA] [AC:P23496] [GN:LACX][OR:Lactococcus lactis] [SR:,subsplactis:Streptococcus lactis] [DE:LACXPROTEIN, PLASMID] [SP:P23496] 141 SPX1211 1211 3872 207 621 374 1.20E-65[LN:S52544] [AC:S52544] [PN:ISL2 protein] [OR:Lactobacillus helveticus]71 SPX1212 1212 3873 107 321 193 4.90E-21 [LN:S52544] [AC:S52544][PN:ISL2 protein] [OR:Lactobacillus helveticus] 71 SPX1213 1213 3874 101303 NO-HIT 6 SPX1214 1214 3875 148 444 88 1.30E-10 [GI:4512375][LN:AB011837] [AC:AB011837] [PN:phosphotransferase system (PTS)][GN:fruA] [OR:Bacillus halodurans] [SR:Bacillus halodurans(strain:C-125) DNA, clone_lib:lambda no.9] 181 SPX1215 1215 3876 4311293 2159 2.90E-302 [GI:2804700] [LN:AF030361] [AC:AF030361][PN:transposase] [OR:Streptococcus pneumoniae] 87 SPX1216 1216 3877 63189 120 2.10E-12 [LN:T30285] [AC:T30285] [PN:hypothetical protein][OR:Streptococcus pneumoniae] 79 SPX1217 1217 3878 417 1251 13952.00E-200 [LN:THD1_LACLA] [AC:Q02145] [GN:ILVA] [OR:Lactococcus lactis][SR:,subsplactis:Streptococcus lactis] [EC:4.2.1.16] [DE:DEAMINASE)][SP:Q02145] 144 SPX1218 1218 3879 119 357 NO-HIT 6 SPX1219 1219 3880 78234 NO-HIT 6 SPX1220 1220 3881 89 267 NO-HIT 6 SPX1221 1221 3882 3411023 1329 9.50E-179 [LN:ILVC_LACLA] [AC:Q02138] [GN:ILVC][OR:Lactococcus lactis] [SR:,subsplactis:Streptococcus lactis][EC:1.1.1.86] [DE:ISOMEROREDUCTASE) (ALPHA-KETO-BETA-HYDROXYLACILREDUCTOISOMERASE)] [SP:Q02138] 199 SPX1222 1222 3883 167 501 4774.10E-62 [LN:ILVN_LACLA] [AC:Q02140] [GN:ILVN] [OR:Lactococcus lactis][SR:,subsplactis:Streptococcus lactis] [EC:4.1.3.18][DE:(ACETOHYDROXY-ACID SYNTHASE SMALL SUBUNIT) (ALS)] [SP:Q02140] 182SPX1223 1223 3884 567 1701 1207 2.30E-266 [LN:ILVB_LACLA] [AC:Q02137][GN:ILVB] [OR:Lactococcus lactis] [SR:,subsplactis:Streptococcus lactis][EC:4.1.3.18] [DE:(ACETOHYDROXY-ACID SYNTHASE LARGE SUBUNIT) (ALS)][SP:Q02137] 182 SPX1224 1224 3885 679 2037 565 7.80E-167 [LN:E69879][AC:E69879] [PN:conserved hypothetical protein yloV] [GN:yloV][CL:Mycoplasma genitalium hypothetical protein MG369] [OR:Bacillussubtilis] 151 SPX1225 1225 3886 63 189 222 4.40E-26 [LN:RL28_BACSU][AC:P37807] [GN:RPMB] [OR:Bacillus subtilis] [DE:50S RIBOSOMAL PROTEINL28] [SP:P37807] 103 SPX1226 1226 3887 82 246 123 5.10E-19 [GI:6760462][LN:AF224467] [AC:AF224467] [PN:putative glycosyl transferase][OR:Haemophilus ducreyi] 100 SPX1227 1227 3888 66 198 157 8.80E-16[GI:6760462] [LN:AF224467] [AC:AF224467] [PN:putative glycosyltransferase] [OR:Haemophilus ducreyi] 100 SPX1228 1228 3889 515 1545 7712.70E-216 [GI:3256222] [LN:SAY14370] [AC:Y14370] [PN:peptide chainrelease factor 3] [GN:RF3] [OR:Staphylococcus aureus] 110 SPX1229 12293890 101 303 190 4.90E-21 [LN:A69795] [AC:A69795] [PN:conservedhypothetical protein yerL] [GN:yerL] [CL:probable glu-tRNAamidotransferase C chain] [OR:Bacillus subtilis] 145 SPX1230 1230 3891489 1467 1333 1.60E-186 [LN:B69795] [AC:B69795] [PN:amidase homologyerM] [GN:yerM] [CL:indoleacetamide hydrolase] [OR:Bacillus subtilis]113 SPX1231 1231 3892 213 639 414 4.30E-94 [LN:T44293] [AC:T44293][PN:hypothetical protein yerN [imported]] [CL:PET112 protein][OR:Bacillus halodurans] 110 SPX1232 1232 3893 269 807 744 4.60E-97[LN:C69795] [AC:C69795] [PN:pet112-like protein homolog yerN] [GN:yerN][CL:PET112 protein] [OR:Bacillus subtilis] 114 SPX1233 1233 3894 3481044 719 1.70E-145 [LN:H69789] [AC:H69789] [PN:L-iditol 2-dehydrogenase,homolog ydjL:sorbitol dehydrogenase homolog] [GN:ydjL] [CL:alcoholdehydrogenase:long-chain alcohol dehydrogenase homology] [OR:Bacillussubtilis] [EC:1.1.1.14] 216 SPX1234 1234 3895 67 201 138 4.80E-14[LN:T30285] [AC:T30285] [PN:hypothetical protein] [OR:Streptococcuspneumoniae] 79 SPX1235 1235 3896 187 561 430 7.10E-54 [LN:EFP_BACSU][AC:P49778] [GN:EFP] [OR:Bacillus subtilis] [DE:ELONGATION FACTOR P(EF-P)] [SP:P49778] 102 SPX1236 1236 3897 130 390 139 8.30E-19[LN:YQHY_BACSU] [AC:P54519] [GN:YQHY] [OR:Bacillus subtilis][DE:HYPOTHETICAL 14.7 KD PROTEIN IN ACCC-FOLD INTERGENIC REGION][SP:P54519] 137 SPX1237 1237 3898 141 423 105 1.00E-12 [GI:6580774][LN:AF088897] [AC:AF088897:AF034613:AF086792:U63733] [PN:N-utilizationsubstance protein B] [GN:nusB] [OR:Zymomonas mobilis] 137 SPX1238 12383899 190 570 948 7.40E-131 [GI:663279] [LN:STRCOMAA] [AC:M36180:L15190][PN:transposase] [OR:Streptococcus pneumoniae] [SR:Streptococcuspneumoniae (strain RX1) DNA] 138 SPX1239 1239 3900 261 783 10751.10E-148 [GI:2804700] [LN:AF030361] [AC:AF030361] [PN:transposase][OR:Streptococcus pneumoniae] 87 SPX1240 1240 3901 278 834 80 9.90E-07[LN:E69787] [AC:E69787] [PN:hypothetical protein ydiL] [GN:ydiL][OR:Bacillus subtilis] 87 SPX1241 1241 3902 84 252 NO-HIT 6 SPX1242 12423903 256 768 653 4.10E-90 [GI:285621] [LN:BACPK] [AC:D13095][PN:undefined open reading frame] [OR:Bacillus stearothermophilus][SR:Bacillus stearothermophilus (strain:NCA1503) DNA] 155 SPX1243 12433904 288 864 602 2.20E-92 [LN:ACCD_SYNP7] [AC:Q54776] [GN:ACCD][OR:Synechococcus sp] [SR:,strain PCC 7942:Anacystis nidulans R2][EC:6.4.1.2] [DE:(EC 6.4.1.2) (ACCASE BETA CHAIN)] [SP:Q54776] 168SPX1244 1244 3905 456 1368 1101 1.50E-181 [LN:A69581] [AC:A69581][PN:acetyl-CoA carboxylase (biotin carboxylase subunit) accC] [GN:accC][CL:biotin carboxylase:biotin carboxylase homology] [OR:Bacillussubtilis] 170 SPX1245 1245 3906 141 423 299 1.60E-49 [LN:D70065][AC:D70065] [PN:(3R)-hydroxymyristoyl-[acyl carrier protein]dehydratase,ywpB] [GN:ywpB] [CL:(3R)-hydroxymyristoyl-[acyl carrierprotein]dehydratase] [OR:Bacillus subtilis] [EC:4.2.1.-] 201 SPX12461246 3907 162 486 248 1.10E-34 [LN:C75558] [AC:C75558] [PN:acetyl-CoAcarboxylase, bitoin carboxyl carrier protein] [GN:DR0118] [CL:biotincarboxyl carrier protein:lipoyl/biotin-binding homology] [OR:Deinococcusradiodurans] 195 SPX1247 1247 3908 93 279 134 1.30E-13 [LN:FAB2_MYCTU][AC:Q10525] [GN:RV2246:MTCY427.27] [OR:Mycobacterium tuberculosis][EC:2.3.1.41] [DE:(BETA-KETOACYL-ACP SYNTHASE 2) (KAS 2)] [SP:Q10525]152 SPX1248 1248 3909 360 1080 477 2.60E-113 [LN:S77464] [AC:S77464][PN:3-oxoacyl-[acyl-carrier-protein]synthase, beta chain:betaketoacyl-acyl carrier protein synthase:protein sll1069:betaketoacyl-acyl carrier protein synthase:protein sll1069] [GN:fabF][OR:Synechocystis sp.] 237 SPX1249 1249 3910 244 732 482 2.10E-76[LN:FABG_CUPLA] [AC:P28643] [GN:CLKR27] [OR:Cuphea lanceolata][EC:1.1.1.100] [DE:(3-KETOACYL-ACYL CARRIER PROTEIN REDUCTASE)][SP:P28643] 138 SPX1250 1250 3911 74 222 81 9.50E-05 [LN:H72482][AC:H72482] [PN:hypothetical protein APE2504] [GN:APE2504] [OR:Aeropyrumpernix] 92 SPX1251 1251 3912 307 921 374 1.00E-85 [LN:B41856][AC:B41856:A42147:S20443:A64853][PN:[acyl-carrier-protein]S-malonyltransferase,] [GN:fabD:tfpA][CL:[acyl-carrier-protein]S-malonyltransferase:[acyl-carrier-protein]S-malonyltransferasehomology] [OR:Escherichia coli] [EC:2.3.1.39] 249 SPX1252 1252 3913 325975 681 5.90E-101 [LN:A72335] [AC:A72335] [PN:conserved hypotheticalprotein] [GN:TM0800] [OR:Thermotoga maritima] 96 SPX1253 1253 3914 75225 80 1.80E-12 [LN:ACP_BACSU] [AC:P80643:P51832] [GN:ACPA:ACPP][OR:Bacillus subtilis] [DE:ACYL CARRIER PROTEIN (ACP)][SP:P80643:P51832] 122 SPX1254 1254 3915 189 567 202 6.90E-38[LN:S75457] [AC:S75457] [PN:beta-ketoacyl-acyl carrier protein synthaseIII:protein slr1511:protein slr1511] [GN:fabH][CL:3-oxoacyl-[acyl-carrier-protein]synthase III] [OR:Synechocystis sp.][SR:PCC 6803, , PCC 6803] [SR:PCC 6803, ] 236 SPX1255 1255 3916 140 420269 1.30E-46 [GI:7416010] [LN:AB025973] [AC:AB025973][PN:3-oxoacyl-[acyl-carrier-protein]synthase III] [GN:accS][OR:Lactobacillus plantarum] [SR:Lactobacillus plantarum (strain:L137)DNA] 177 SPX1256 1256 3917 66 198 NO-HIT 6 SPX1257 1257 3918 145 435 1395.00E-12 [GI:4139249] [LN:AF110185] [AC:AF110185] [PN:unknown][OR:Burkholderia pseudomallei] 84 SPX1258 1258 3919 66 198 NO-HIT 6SPX1259 1259 3920 98 294 138 7.10E-13 [GI:3253198] [LN:AF029714][AC:AF029714:Z71175] [PN:PhaB] [GN:phaB] [OR:Pseudomonas putida] 91SPX1260 1260 3921 76 228 156 9.00E-18 [GI:1914870] [LN:SPZ82001][AC:Z82001] [PN:unknown] [OR:Streptococcus pneumoniae] 81 SPX1261 12613922 455 1365 1240 6.10E-166 [LN:A69763] [AC:A69763] [PN:homoserinedehydrogenase homolog yclM] [GN:yclM] [CL:aspartate kinase:aspartatekinase homology] [OR:Bacillus subtilis] 147 SPX1262 1262 3923 124 372493 2.80E-64 [GI:5669858] [LN:AF130465] [AC:AF130465] [PN:unknown][GN:manO] [OR:Streptococcus salivarius] 93 SPX1263 1263 3924 375 1125564 8.90E-141 [LN:SYS_BACSU] [AC:P37464] [GN:SERS] [OR:Bacillussubtilis] [EC:6.1.1.11] [DE:SERYL-TRNA SYNTHETASE, (SERINE--TRNA LIGASE)(SERRS)] [SP:P37464] 145 SPX1264 1264 3925 91 273 101 6.30E-08[LN:SYS_MYCGE] [AC:P47251] [GN:SERS:MG005] [OR:Mycoplasma genitalium][EC:6.1.1.11] [DE:SERYL-TRNA SYNTHETASE, (SERINE--TRNA LIGASE) (SERRS)][SP:P47251] 155 SPX1265 1265 3926 304 912 NO-HIT 6 SPX1266 1266 3927 69207 NO-HIT 6 SPX1267 1267 3928 183 549 217 2.40E-57 [GI:7379894][LN:NMA4Z2491] [AC:AL162755:AL157959] [PN:hypothetical protein NMA1203][GN:NMA1203] [OR:Neisseria meningitidis] 125 SPX1268 1268 3929 441 1323611 6.80E-118 [LN:D71327] [AC:D71327] [PN:probable D-alanine glycinepermease (dagA)] [GN:TP0414] [CL:sodium-dependent D-alanine/glycinetransport protein] [OR:Treponema pallidum subsp. pallidum] [SR:,syphilis spirochete] 210 SPX1269 1269 3930 779 2337 671 5.70E-155[LN:MUS2_BACSU] [AC:P94545] [GN:MUTS2] [OR:Bacillus subtilis] [DE:MUTS2PROTEIN] [SP:P94545] 92 SPX1270 1270 3931 251 753 175 7.10E-43[GI:6746427] [LN:AF179847] [AC:AF179847] [PN:putative transposase][OR:Lactococcus lactis] 90 SPX1271 1271 3932 65 195 NO-HIT 6 SPX12721272 3933 182 546 107 1.20E-15 [GI:3849798] [LN:U91581][AC:U91581:U04057] [PN:putative transposase] [GN:tpase] [OR:Lactococcuslactis subsp. lactis] 118 SPX1273 1273 3934 183 549 95 4.30E-13[LN:B69985] [AC:B69985] [PN:hypothetical protein yshB] [GN:yshB][OR:Bacillus subtilis] 87 SPX1274 1274 3935 104 312 NO-HIT 6 SPX12751275 3936 294 882 1444 8.00E-194 [LN:RNH2_STRPN] [AC:O07874] [GN:RNHB][OR:Streptococcus pneumoniae] [EC:3.1.26.4] [DE:RIBONUCLEASE HII, (RNASEHII)] [SP:O07874] 130 SPX1276 1276 3937 205 615 1065 6.70E-145[LN:LEP_STRPN] [AC:O07344] [GN:LEPB:SPI] [OR:Streptococcus pneumoniae][EC:3.4.21.89] [DE:SIGNAL PEPTIDASE I, (SPASE I) (LEADER PEPTIDASE I)][SP:O07344] 155 SPX1277 1277 3938 93 279 NO-HIT 6 SPX1278 1278 3939 7892367 738 5.80E-165 [LN:A69979] [AC:A69979] [PN:conjugation transferprotein homolog yrrC] [GN:yrrC] [OR:Bacillus subtilis] 103 SPX1279 12793940 428 1284 1691 1.40E-223 [GI:3549287] [LN:AF073922] [AC:AF073922][PN:RopA] [GN:ropA] [OR:Streptococcus pyogenes] 88 SPX1280 1280 3941 3791137 1350 2.20E-182 [LN:MTLD_STRMU] [AC:Q02418] [GN:MTLD][OR:Streptococcus mutans] [EC:1.1.1.17] [DE:MANNITOL-1-PHOSPHATE5-DEHYDROGENASE,] [SP:Q02418] 134 SPX1281 1281 3942 146 438 544 5.30E-71[LN:PTMA_STRMU] [AC:Q02420] [GN:MTLF] [OR:Streptococcus mutans][EC:2.7.1.69] [DE:(EC 2.7.1.69) (EIII-MTL)] [SP:Q02420] 119 SPX1282 12823943 652 1956 392 1.00E-47 [LN:YMTF_STRMU] [AC:Q02425] [OR:Streptococcusmutans] [DE:HYPOTHETICAL PROTEIN IN MTLF 5′REGION (ORFX) (FRAGMENT)][SP:Q02425] 126 SPX1283 1283 3944 596 1788 1099 4.90E-194[LN:PTMB_BACST] [AC:P50852] [GN:MTLA] [OR:Bacillus stearothermophilus][EC:2.7.1.69] [DE:(EC 2.7.1.69) (EII-MTL)] [SP:P50852] 125 SPX1284 12843945 67 201 NO-HIT 6 SPX1285 1285 3946 191 573 422 2.30E-53 [LN:B30868][AC:B30868] [PN:hypothetical protein 1] [OR:Streptococcus agalactiae] 81SPX1286 1286 3947 278 834 582 1.50E-140 [LN:A33595] [AC:A33595:A30868][PN:probable transposase] [CL:transposase IS3] [OR:Streptococcusagalactiae] 107 SPX1287 1287 3948 341 1023 1142 5.00E-219 [GI:1914875][LN:SPZ82002] [AC:Z82002] [PN:PCPC] [GN:pcpC] [FN:unknown][OR:Streptococcus pneumoniae] 101 SPX1288 1288 3949 98 294 194 3.40E-25[GI:4586910] [LN:AB017447] [AC:AB017447] [PN:protective antigen SpaA.1][OR:Erysipelothrix rhusiopathiae] [SR:Erysipelothrix rhusiopathiae(strain:Fujisawa) DNA] 161 SPX1289 1289 3950 219 657 104 1.50E-08[LN:S25140] [AC:S25140] [PN:serine proteinase homolog][CL:staphylococcal serine proteinase] [OR:Enterococcus faecalis] 119SPX1290 1290 3951 80 240 296 8.20E-35 [GI:1914874] [LN:SPZ82002][AC:Z82002] [PN:unknown] [OR:Streptococcus pneumoniae] 81 SPX1291 12913952 91 273 146 3.20E-14 [GI:4584089] [LN:BAJ10128] [AC:AJ010128][PN:DNA alkylation repair enzyme] [GN:alkD] [FN:complements DNAalkylation repair deficiency] [OR:Bacillus cereus] 155 SPX1292 1292 395385 255 102 2.90E-08 [GI:4584089] [LN:BAJ10128] [AC:AJ010128] [PN:DNAalkylation repair enzyme] [GN:alkD] [FN:complements DNA alkylationrepair deficiency] [OR:Bacillus cereus] 155 SPX1293 1293 3954 211 6331040 1.50E-139 [GI:5830527] [LN:SPAJ6393] [AC:AJ006393] [PN:responseregulator] [GN:rr03] [OR:Streptococcus pneumoniae] 104 SPX1294 1294 3955332 996 1603 3.60E-220 [GI:5830526] [LN:SPAJ6393] [AC:AJ006393][PN:histidine kinase] [GN:hk03] [OR:Streptococcus pneumoniae] 102SPX1295 1295 3956 233 699 104 1.50E-11 [LN:G70045] [AC:G70045][PN:hypothetical protein yvqF] [GN:yvqF] [OR:Bacillus subtilis] 87SPX1296 1296 3957 337 1011 151 6.20E-42 [LN:D75084] [AC:D75084][PN:carotenoid biosynthetic gene erwcrts related PAB1662] [GN:PAB1662][CL:carotenoid biosynthesis protein homolog] [OR:Pyrococcus abyssi] 162SPX1297 1297 3958 336 1008 67 0.00053 [LN:KIME_METJA] [AC:Q58487][GN:MJ1087] [OR:Methanococcus jannaschii] [EC:2.7.1.36] [DE:MEVALONATEKINASE, (MK)] [SP:Q58487] 126 SPX1298 1298 3959 345 1035 141 5.90E-28[GI:6625790] [LN:AF203779] [AC:AF203779] [PN:diphosphomevalonatedecarboxylase MVD1] [GN:MVD1] [OR:Candida albicans] 116 SPX1299 12993960 293 879 134 1.60E-20 [LN:F72474] [AC:F72474] [PN:probablemevalonate kinase APE2439] [GN:APE2439] [OR:Aeropyrum pernix] 98 SPX13001300 3961 110 330 193 8.50E-21 [GI:1914875] [LN:SPZ82002] [AC:Z82002][PN:PCPC] [GN:pcpC] [FN:unknown] [OR:Streptococcus pneumoniae] 101SPX1301 1301 3962 292 876 NO-HIT 6 SPX1302 1302 3963 411 1233 974.90E-10 [GI:3582221] [LN:AE001272] [AC:AE001272] [PN:conservedhypothetical protein] [GN:ORF00049] [OR:Lactococcus lactis] 114 SPX13031303 3964 333 999 402 1.50E-124 [GI:1914875] [LN:SPZ82002] [AC:Z82002][PN:PCPC] [GN:pcpC] [FN:unknown] [OR:Streptococcus pneumoniae] 101SPX1304 1304 3965 371 1113 289 1.70E-89 [GI:1914875] [LN:SPZ82002][AC:Z82002] [PN:PCPC] [GN:pcpC] [FN:unknown] [OR:Streptococcuspneumoniae] 101 SPX1305 1305 3966 230 690 212 7.30E-56 [GI:3599371][LN:AF082668] [AC:AF082668] [PN:CsrR] [GN:csrR] [FN:negative regulatorof hyaluronic acid capsule] [OR:Streptococcus pyogenes] 139 SPX1306 13063967 458 1374 801 5.10E-226 [GI:3033358] [LN:LLU74322] [AC:U74322][PN:6-phosphogluconate dehydrogenase] [OR:Lactococcus lactis] 100SPX1307 1307 3968 465 1395 109 1.10E-06 [GI:1684847] [LN:HSU77718][AC:U77718] [PN:pinin] [OR:Homo sapiens] [SR:human] 78 SPX1308 1308 3969386 1158 678 1.20E-133 [LN:YPSC_BACSU] [AC:P50840] [GN:YPSC][OR:Bacillus subtilis] [DE:HYPOTHETICAL 43.5 KD PROTEIN IN COTD-KDUDINTERGENIC REGION PRECURSOR] [SP:P50840] 147 SPX1309 1309 3970 110 330166 6.70E-18 [LN:YPSB_BACSU] [AC:P50839] [GN:YPSB] [OR:Bacillussubtilis] [DE:HYPOTHETICAL 11.6 KD PROTEIN IN COTD-KDUD INTERGENICREGION] [SP:P50839] 137 SPX1310 1310 3971 176 528 147 8.20E-19[LN:YPSA_BACSU] [AC:P50838] [GN:YPSA] [OR:Bacillus subtilis][DE:HYPOTHETICAL 21.1 KD PROTEIN IN COTD-KDUD INTERGENIC REGION][SP:P50838] 137 SPX1311 1311 3972 199 597 1043 3.40E-141 [LN:YPOA_STRPN][AC:P38034] [OR:Streptococcus pneumoniae] [DE:HYPOTHETICAL 23.1 KDPROTEIN IN PONA 5′REGION] [SP:P38034] 120 SPX1312 1312 3973 720 21603734 0 [GI:6563337] [LN:AF210745] [AC:AF210745] [PN:penicillin-bindingprotein 1A] [GN:pbp1a] [OR:Streptococcus pneumoniae] 116 SPX1313 13133974 68 204 NO-HIT 6 SPX1314 1314 3975 1768 5304 1762 9.10E-232[GI:1658320] [LN:SPDEXCAP] [AC:Z47210] [GN:orf] [OR:Streptococcuspneumoniae] 77 SPX1315 1315 3976 661 1983 3378 0 LN:ALIA_STRPN][AC:P35592:Q54782:O54620:O52228] [GN:ALIA:EXP1:PLPA] [OR:Streptococcuspneumoniae] [DE:OLIGOPEPTIDE-BINDING PROTEIN ALIA PRECURSOR (EXPORTEDPROTEIN 1)] [SP:P35592:Q54782:O54620:O52228] 201 SPX1316 1316 3977 78234 87 0.00034 [GI:5824139] [LN:POL245436][AC:AJ245436:J04618:J04619:S50571:X52935:X65936] [PN:hypotheticalprotein, 57.8 kD] [OR:Pseudomonas putida] 137 SPX1317 1317 3978 150 45094 3.20E-15 [LN:Y4HP_RHISN] [AC:P50360] [GN:Y4HP] [OR:Rhizobium sp][SR:,strain NGR234] [DE:HYPOTHETICAL 61.7 KD PROTEIN Y4HP] [SP:P50360]128 SPX1318 1318 3979 58 174 NO-HIT 6 SPX1319 1319 3980 86 258 808.90E-06 [LN:Y4HP_RHISN] [AC:P50360] [GN:Y4HP] [OR:Rhizobium sp][SR:,strain NGR234] [DE:HYPOTHETICAL 61.7 KD PROTEIN Y4HP] [SP:P50360]128 SPX1320 1320 3981 143 429 84 9.20E-08 [GI:6009407] [LN:AB024946][AC:AB024946] [GN:orf31] [OR:Escherichia coli] [SR:Escherichia coli(sub_species:enteropathogenic, strain:B171] 140 SPX1321 1321 3982 284852 1480 1.00E-198 [GI:2804705] [LN:AF030362] [AC:AF030362][PN:dTDP-L-rhamnose synthase] [GN:cpsO] [OR:Streptococcus pneumoniae]110 SPX1322 1322 3983 350 1050 1853 2.90E-249 [GI:4200435] [LN:AF026471][AC:AF026471] [PN:Cps2N] [GN:cps2N] [OR:Streptococcus pneumoniae] 92SPX1323 1323 3984 199 597 1027 4.50E-137 [GI:3907611] [LN:AF094575][AC:AF094575] [PN:dTDP-4-keto-6-deoxyglucose-3,5-epimerase] [GN:cps19aM][OR:Streptococcus pneumoniae] 131 SPX1324 1324 3985 290 870 14307.20E-193 [GI:4406249] [LN:AF105113] [AC:AF105113][PN:glucose-1-phosphate thymidylyl transferase] [GN:cps19AL][OR:Streptococcus pneumoniae] 131 SPX1325 1325 3986 476 1428 20173.10E-287 [GI:3907608] [LN:AF094575] [AC:AF094575] [PN:putative repeatunit transporter Cps19aJ] [GN:cps19aJ] [OR:Streptococcus pneumoniae] 129SPX1326 1326 3987 95 285 NO-HIT 6 SPX1327 1327 3988 448 1344 1486.90E-31 [GI:3907607] [LN:AF094575] [AC:AF094575] [PN:polysaccharidepolymerase Cps19aI] [GN:cps19aI] [OR:Streptococcus pneumoniae] 122SPX1328 1328 3989 329 987 178 2.00E-31 [LN:T00087] [AC:T00087][PN:rhamnosyltransferase] [GN:rgpBc] [OR:Streptococcus mutans] 86SPX1329 1329 3990 242 726 93 1.90E-06 [LN:T35395] [AC:T35395][PN:probable transferase] [GN:SC6A5.04] [OR:Streptomyces coelicolor] 92SPX1330 1330 3991 186 558 154 3.00E-14 [GI:2209209] [LN:AF004325][AC:AF004325] [PN:unknown] [GN:cps19bG] [OR:Streptococcus pneumoniae] 96SPX1331 1331 3992 315 945 96 6.50E-16 [GI:3132871] [LN:AF019375][AC:AF019375] [PN:UDP-glucose:(glucosyl) LPS] [GN:waaR] [OR:Escherichiacoli] 104 SPX1332 1332 3993 456 1368 1141 0 [GI:3907603] [LN:AF094575][AC:AF094575] [PN:glucosyl-1-phosphate transferase Cps19aE] [GN:cps19aE][OR:Streptococcus pneumoniae] 129 SPX1333 1333 3994 227 681 10554.60E-145 [GI:3907602] [LN:AF094575] [AC:AF094575] [PN:Cps19aD][GN:cps19aD] [FN:chain length regulation and export] [OR:Streptococcuspneumoniae] 136 SPX1334 1334 3995 232 696 1061 2.00E-141 [GI:3907601][LN:AF094575] [AC:AF094575] [PN:Cps19aC] [GN:cps19aC] [FN:chain lengthregulation and export] [OR:Streptococcus pneumoniae] 136 SPX1335 13353996 260 780 1195 2.90E-162 [GI:3907600] [LN:AF094575] [AC:AF094575][PN:Cps19aB] [GN:cps19aB] [OR:Streptococcus pneumoniae] 96 SPX1336 13363997 485 1455 2238 0 [GI:3550627] [LN:SPAJ6986] [AC:AJ006986][GN:cap33fA] [OR:Streptococcus pneumoniae] 83 SPX1337 1337 3998 358 10741690 9.20E-228 [LN:TRA2_STRPN] [AC:Q54513] [OR:Streptococcus pneumoniae][DE:TRANSPOSASE FOR INSERTION SEQUENCE IS1202] [SP:Q54513] 116 SPX13381338 3999 120 360 581 6.60E-75 [LN:TRA2_STRPN] [AC:Q54513][OR:Streptococcus pneumoniae] [DE:TRANSPOSASE FOR INSERTION SEQUENCEIS1202] [SP:Q54513] 116 SPX1339 1339 4000 317 951 267 3.80E-61[GI:6332767] [LN:AB033763] [AC:AB033763:AB014419:AB014429:AB014439][PN:hypothetical protein] [OR:Staphylococcus aureus] [SR:Staphylococcusaureus (strain:NCTC10442) DNA, clone_lib:Lambda das] 194 SPX1340 13404001 179 537 551 1.10E-70 [LN:B30868] [AC:B30868] [PN:hypotheticalprotein 1] [OR:Streptococcus agalactiae] 81 SPX1341 1341 4002 161 483550 2.00E-80 [LN:A33595] [AC:A33595:A30868] [PN:probable transposase][CL:transposase IS3] [OR:Streptococcus agalactiae] 107 SPX1342 1342 4003278 834 587 1.60E-140 [LN:A33595] [AC:A33595:A30868] [PN:probabletransposase] [CL:transposase IS3] [OR:Streptococcus agalactiae] 107SPX1343 1343 4004 537 1611 2499 0 [GI:3320387] [LN:AF030373][AC:AF030373] [PN:alpha, 1-6-glucosidase] [GN:dexB] [OR:Streptococcuspneumoniae] 110 SPX1344 1344 4005 495 1485 NO-HIT 6 SPX1345 1345 4006161 483 288 9.40E-46 [LN:D75280] [AC:D75280] [PN:conserved hypotheticalprotein] [GN:DR2387] [CL:conserved hypothetical protein HI0491][OR:Deinococcus radiodurans] 143 SPX1346 1346 4007 702 2106 2049 0[GI:871784] [LN:BOVCLPAB] [AC:L34677] [PN:Clp-like ATP-dependentprotease binding subunit] [OR:Bos taurus] [SR:Bos taurus calf thymuscDNA to mRNA] 147 SPX1347 1347 4008 80 240 NO-HIT 6 SPX1348 1348 4009327 981 1619 8.40E-229 [GI:4009489] [LN:AF068903] [AC:AF068903][PN:undecaprenyl-phosphate-UDP-MurNAc-pentapeptide] [GN:mraY][OR:Streptococcus pneumoniae] 132 SPX1349 1349 4010 751 2253 3812 0[LN:PBPX_STRPN] [AC:P14677] [GN:PBPX] [OR:Streptococcus pneumoniae][DE:PENICILLIN-BINDING PROTEIN 2X (PBP-2X) (PBP2X)] [SP:P14677] 131SPX1350 1350 4011 106 318 505 1.40E-65 [GI:4009487] [LN:AF068903][AC:AF068903] [PN:YllD] [GN:yllD] [OR:Streptococcus pneumoniae] 90SPX1351 1351 4012 317 951 1604 2.70E-217 [GI:4009486] [LN:AF068903][AC:AF068903] [PN:YllC] [GN:yllC] [OR:Streptococcus pneumoniae] 90SPX1352 1352 4013 65 195 323 1.20E-40 [GI:1536960] [LN:SOORFS][AC:Z79691] [GN:yorfE] [FN:putative transcription regulator][OR:Streptococcus pneumoniae] 115 SPX1353 1353 4014 142 426 291 1.40E-36[GI:1524349] [LN:SOORFS] [AC:Z79691] [PN:OrfC] [GN:yorfC][OR:Streptococcus pneumoniae] 87 SPX1354 1354 4015 94 282 NO-HIT 6SPX1355 1355 4016 85 255 178 5.70E-20 [GI:1536959] [LN:SOORFS][AC:Z79691] [PN:OrfB] [GN:yorfb] [OR:Streptococcus pneumoniae] 87SPX1356 1356 4017 81 243 391 2.00E-51 [GI:1536959] [LN:SOORFS][AC:Z79691] [PN:OrfB] [GN:yorfb] [OR:Streptococcus pneumoniae] 87SPX1357 1357 4018 112 336 219 4.90E-27 [GI:1536959] [LN:SOORFS][AC:Z79691] [PN:OrfB] [GN:yorfb] [OR:Streptococcus pneumoniae] 87SPX1358 1358 4019 64 192 111 4.30E-10 [GI:1536959] [LN:SOORFS][AC:Z79691] [PN:OrfB] [GN:yorfb] [OR:Streptococcus pneumoniae] 87SPX1359 1359 4020 334 1002 1703 2.00E-229 [GI:1536958] [LN:SOORFS][AC:Z79691] [PN:RegR] [GN:regR] [FN:putative transcription regulator,member GalR] [OR:Streptococcus pneumoniae] 139 SPX1360 1360 4021 6341902 1094 3.90E-148 [GI:1524347] [LN:SOORFS] [AC:Z79691] [PN:OrfA][GN:yorfA] [OR:Streptococcus pneumoniae] 87 SPX1361 1361 4022 98 294 967.80E-07 [LN:D70408] [AC:D70408] [PN:conserved hypothetical proteinaq_1254] [GN:aq_1254] [CL:yajC protein] [OR:Aquifex aeolicus] 120SPX1362 1362 4023 273 819 268 3.50E-51 [LN:PTPD_ECOLI] [AC:P42911][GN:AGAD] [OR:Escherichia coli] [DE:ENZYME II, D COMPONENT)] [SP:P42911]102 SPX1363 1363 4024 260 780 170 4.30E-27 [GI:1732200] [LN:VFU65015][AC:U65015] [PN:PTS permease for mannose subunit IIPMan] [GN:manY][OR:Vibrio furnissii] 115 SPX1364 1364 4025 164 492 286 3.40E-44[LN:PTPV_ECOLI] [AC:P42904:P76669] [GN:AGAV] [OR:Escherichia coli][EC:2.7.1.69] [DE:ENZYME II, B COMPONENT 2),] [SP:P42904:P76669] 133SPX1365 1365 4026 336 1008 475 2.70E-95 [GI:5869507] [LN:AB019619][AC:AB019619] [PN:unsaturated glucuronyl hydrolase] [GN:ugl][OR:Bacillus sp. GL1] [SR:Bacillus sp. GL1 (strain:GL1) DNA] 148 SPX13661366 4027 146 438 NO-HIT 6 SPX1367 1367 4028 145 435 129 3.30E-17[GI:5669855] [LN:AF130465] [AC:AF130465] [PN:mannose-specificphosphotransferase system] [GN:manL] [OR:Streptococcus salivarius] 128SPX1368 1368 4029 218 654 436 1.40E-55 [LN:YJGU_ECOLI] [AC:P39345][GN:YJGU] [OR:Escherichia coli] [EC:1.-.-.-] [DE:(EC 1.-.-.-)][SP:P39345] 102 SPX1369 1369 4030 125 375 NO-HIT 6 SPX1370 1370 4031 98294 169 2.50E-19 [LN:YJGU_ECOLI] [AC:P39345] [GN:YJGU] [OR:Escherichiacoli] [EC:1.-.-.-] [DE:(EC 1.-.-.-)] [SP:P39345] 102 SPX1371 1371 4032214 642 NO-HIT 6 SPX1372 1372 4033 334 1002 317 1.00E-46 [LN:G72422][AC:G72422] [PN:2-keto-3-deoxygluconate kinase] [GN:TM0067][CL:ribokinase] [OR:Thermotoga maritima] 112 SPX1373 1373 4034 210 630271 6.10E-46 [LN:F72422] [AC:F72422][PN:2-dehydro-3-deoxyphosphogluconate aldolase/4-hydroxy-2-oxoglutaratealdolase] [GN:TM0066] [CL:2-dehydro-3-deoxyphosphogluconate aldolase][OR:Thermotoga maritima] 190 SPX1374 1374 4035 118 354 264 1.50E-50[GI:1841332] [LN:D64071] [AC:D64071] [PN:putative protein of unknownfunction] [OR:Actinobacillus actinomycetemcomitans] [SR:Actinobacillusactinomycetemcomitans (strain:Y4) DNA] 178 SPX1375 1375 4036 1079 32374863 0 [LN:HYSA_STRPN] [AC:Q54873:Q54874] [OR:Streptococcus pneumoniae][EC:4.2.2.1] [DE:HYALURONATE LYASE PRECURSOR, (HYALURONIDASE) (HYASE)][SP:Q54873:Q54874] 156 SPX1376 1376 4037 159 477 482 1.90E-62[GI:2598550] [LN:LLAJ109] [AC:AJ000109] [PN:gluthatione peroxidase][GN:gpo] [OR:Lactococcus lactis] 100 SPX1377 1377 4038 738 2214 1814.50E-33 [GI:6686567] [LN:AAC252161] [AC:AJ252161] [PN:putativealpha-glucosidase] [GN:glcA] [OR:Alicyclobacillus acidocaldarius] 120SPX1378 1378 4039 61 183 NO-HIT 6 SPX1379 1379 4040 449 1347 2313.40E-63 [LN:PTCC_BACST] [AC:Q45400] [GN:CELB] [OR:Bacillusstearothermophilus] [DE:PERMEASE IIC COMPONENT) (PHOSPHOTRANSFERASEENZYME II, C COMPONENT)] [SP:Q45400] 157 SPX1380 1380 4041 169 507NO-HIT 6 SPX1381 1381 4042 105 315 234 2.00E-27 [LN:PTCA_BACSU][AC:P46319] [GN:CELC:LICA] [OR:Bacillus subtilis] [EC:2.7.1.69] [DE:(EC2.7.1.69) (EIII-CEL)] [SP:P46319] 121 SPX1382 1382 4043 660 1980 1389.20E-51 [LN:CELR_BACSU] [AC:P46321] [GN:CELR:LICR] [OR:Bacillussubtilis] [DE:PUTATIVE CEL OPERON REGULATOR] [SP:P46321] 112 SPX13831383 4044 114 342 84 2.40E-08 [LN:PTCB_BACST] [AC:Q45399] [GN:CELA][OR:Bacillus stearothermophilus] [EC:2.7.1.69] [DE:(EC 2.7.1.69)][SP:Q45399] 115 SPX1384 1384 4045 80 240 142 1.20E-15 [LN:Y110_METJA][AC:Q57574] [GN:MJ0110] [OR:Methanococcus jannaschii] [DE:HYPOTHETICALPROTEIN MJ0110] [SP:Q57574] 114 SPX1385 1385 4046 493 1479 797 2.50E-225[LN:JE0395] [AC:JE0395] [PN:phospho-beta-galactosidase I][CL:Agrobacterium beta-glucosidase] [OR:Lactobacillus gasseri] 120SPX1386 1386 4047 122 366 NO-HIT 6 SPX1387 1387 4048 69 207 359 2.90E-46[GI:5019553] [LN:SPN239004] [AC:AJ239004] [PN:putative transposase][OR:Streptococcus pneumoniae] 97 SPX1388 1388 4049 131 393 456 1.30E-58[LN:RS9_BACST] [AC:P07842] [GN:RPSI] [OR:Bacillus stearothermophilus][DE:30S RIBOSOMAL PROTEIN S9 (BS10)] [SP:P07842] 118 SPX1389 1389 4050149 447 487 2.30E-62 [LN:RL13_STACA] [AC:Q00990] [GN:RPLM][OR:Staphylococcus carnosus] [DE:50S RIBOSOMAL PROTEIN L13] [SP:Q00990]109 SPX1390 1390 4051 122 366 NO-HIT 6 SPX1391 1391 4052 106 318 NO-HIT6 SPX1392 1392 4053 131 393 630 8.40E-84 [LN:SULD_STRPN][AC:P22291:O33697] [GN:SULD] [OR:Streptococcus pneumoniae][EC:4.1.2.25:2.7.6.3] [DE:HYDROXYMETHYL-7,8-DIHYDROPTERINPYROPHOSPHOKINASE) (PPPK)]] [SP:P22291:O33697] 181 SPX1393 1393 4054 170510 834 1.40E-111 [LN:A36704] [AC:A36704] [PN:bifunctional folatebiosynthesis enzyme sulD:6-hydroxymethyl-7,8-dihydropterinpyrophosphokinase:7, 8-dihydro-6-hydroxymethylpterin pyrophosphokinase][GN:sulD] [OR:Streptococcus pneumoniae] 220 SPX1394 1394 4055 185 555938 4.90E-127 [LN:GCH1_STRPN] [AC:P51595] [GN:SULC] [OR:Streptococcuspneumoniae] [EC:3.5.4.16] [DE:GTP CYCLOHYDROLASE I, (GTP-CH-I)][SP:P51595] 133 SPX1395 1395 4056 441 1323 2219 0 [GI:564018][LN:SPU16156] [AC:U16156:M17362:M58706] [PN:dihydrofolate synthetase][GN:sulB] [FN:folate biosynthesis] [OR:Streptococcus pneumoniae] 146SPX1396 1396 4057 327 981 1485 7.00E-201 [LN:DHPS_STRPN] [AC:P05382][GN:SULA] [OR:Streptococcus pneumoniae] [EC:2.5.1.15][DE:PYROPHOSPHORYLASE)] [SP:P05382] 117 SPX1397 1397 4058 236 708 1433.00E-13 [GI:1402529] [LN:D78257] [AC:D78257] [PN:ORF8] [GN:orf8][OR:Enterococcus faecalis] [SR:Enterococcus faecalis plasmid:pYI17 DNA]128 SPX1398 1398 4059 62 186 NO-HIT 6 SPX1399 1399 4060 494 1482 4471.70E-116 [GI:6624219] [LN:AB023289] [AC:AB023289] [GN:ORFX][OR:Pseudomonas fluorescens] [SR:Pseudomonas fluorescens (strain:No.33)DNA] 127 SPX1400 1400 4061 271 813 199 8.70E-36 [LN:F69841] [AC:F69841][PN:conserved hypothetical protein yitU] [GN:yitU] [CL:Methanobacteriumthermoautotrophicum conserved hypothetical protein MTH1071] [OR:Bacillussubtilis] 178 SPX1401 1401 4062 311 933 861 2.70E-156 [GI:7379448][LN:NMA3Z2491] [AC:AL162754:AL157959] [PN:putative alcoholdehydrogenase] [GN:adhA] [OR:Neisseria meningitidis] 124 SPX1402 14024063 333 999 795 2.40E-188 [GI:5669855] [LN:AF130465] [AC:AF130465][PN:mannose-specific phosphotransferase system] [GN:manL][OR:Streptococcus salivarius] 128 SPX1403 1403 4064 268 804 9741.10E-144 [GI:5669856] [LN:AF130465] [AC:AF130465] [PN:mannose-specificphosphotransferase system] [GN:manM] [OR:Streptococcus salivarius] 128SPX1404 1404 4065 304 912 1157 3.60E-158 [GI:5669857] [LN:AF130465][AC:AF130465] [PN:mannose-specific phosphotransferase system] [GN:manN][OR:Streptococcus salivarius] 128 SPX1405 1405 4066 445 1335 19004.00E-256 [LN:PEPC_STRTR] [AC:Q56115] [GN:PEPC] [OR:Streptococcusthermophilus] [EC:3.4.22.-] [DE:AMINOPEPTIDASE C,] [SP:Q56115] 120SPX1406 1406 4067 241 723 223 1.50E-59 [GI:7328274] [LN:SAY14816][AC:Y14816] [PN:hypothetical protein] [GN:ORF231] [OR:Staphylococcusaureus] 103 SPX1407 1407 4068 137 411 328 2.80E-41 [LN:T30285][AC:T30285] [PN:hypothetical protein] [OR:Streptococcus pneumoniae] 79SPX1408 1408 4069 77 231 NO-HIT 6 SPX1409 1409 4070 77 231 154 1.90E-17[LN:B69770] [AC:B69770] [PN:conserved hypothetical protein ydaS][GN:ydaS] [OR:Bacillus subtilis] 97 SPX1410 1410 4071 414 1242 17926.20E-241 [GI:4731022] [LN:AF102860] [AC:AF102860] [PN:aminopeptidasePepS] [GN:pepS] [OR:Streptococcus thermophilus] 107 SPX1411 1411 4072 60180 NO-HIT 6 SPX1412 1412 4073 77 231 NO-HIT 6 SPX1413 1413 4074 93 279110 1.90E-19 [LN:B71883] [AC:B71883] [PN:hypothetical protein jhp0831][GN:jhp0831] [CL:conserved hypothetical protein HI0711] [OR:Helicobacterpylori] [SR:strain J99, , strain J99] [SR:strain J99, ] 188 SPX1414 14144075 88 264 80 0.00012 [LN:DINJ_ECOLI] [AC:Q47150] [GN:DINJ][OR:Escherichia coli] [DE:DNA-DAMAGE-INDUCIBLE PROTEIN J] [SP:Q47150]107 SPX1415 1415 4076 1464 4392 1689 0 [GI:143342] [LN:BACPOLC][AC:M22996] [GN:polC] [OR:Bacillus subtilis] [SR:B.subtilis SB19 DNA,clone PRO10] 109 SPX1416 1416 4077 694 2082 2833 0 [LN:T44380][AC:T44380] [PN:translation elongation factor EF-G fus [imported]][GN:fus] [CL:translation elongation factor G:translation elongationfactor Tu homology] [OR:Bacillus halodurans] 191 SPX1417 1417 4078 119357 86 5.20E-10 [LN:YHA2_EIKCO] [AC:P35649] [OR:Eikenella corrodens][DE:HYPOTHETICAL 66.3 KD PROTEIN IN HAG2 5′REGION] [SP:P35649] 115SPX1418 1418 4079 150 450 88 1.30E-08 [LN:YHA2_EIKCO] [AC:P35649][OR:Eikenella corrodens] [DE:HYPOTHETICAL 66.3 KD PROTEIN IN HAG25′REGION] [SP:P35649] 115 SPX1419 1419 4080 144 432 173 1.90E-17[GI:7576785] [LN:AF214675] [AC:AF214675] [PN:unknown in vivo-inducedprotein 131-19] [OR:Pseudomonas aeruginosa] 112 SPX1420 1420 4081 157471 633 1.10E-83 [LN:F69699] [AC:F69699:S11357] [PN:ribosomal protein S7(rpsG):ribosomal protein BS7] [GN:rpsG] [CL:Escherichia coli ribosomalprotein S7] [OR:Bacillus subtilis] 161 SPX1421 1421 4082 138 414 6991.70E-91 [LN:RS12_STRPN] [AC:P30891] [GN:RPSL:STR] [OR:Streptococcuspneumoniae] [DE:30S RIBOSOMAL PROTEIN S12] [SP:P30891] 114 SPX1422 14224083 1205 3615 1478 0 [GI:1665738] [LN:D78258] [AC:D78258] [PN:alkalineamylopullulanase] [OR:Bacillus sp.] [SR:Bacillus sp. (strain:KSM-1378)DNA] 125 SPX1423 1423 4084 308 924 655 1.70E-115 [GI:2735505][LN:SCU96107] [AC:U96107] [PN:N5,N10-methylenetetrahydromethanopterin][OR:Staphylococcus carnosus] 114 SPX1424 1424 4085 603 1809 9633.70E-194 [LN:B69633] [AC:B69633] [PN:glutamine--fructose-6-phosphatetransaminase (isomerizing), glmS] [GN:glmS][CL:glutamine--fructose-6-phosphate aminotransferase (isomerizing)][OR:Bacillus subtilis] [EC:2.6.1.16] 210 SPX1425 1425 4086 460 1380 8512.00E-207 [LN:D69785] [AC:D69785] [PN:beta-glucosidase homolog ydhP][GN:ydhP] [CL:Agrobacterium beta-glucosidase] [OR:Bacillus subtilis] 127SPX1426 1426 4087 347 1041 298 1.30E-82 [LN:G69682] [AC:G69682][PN:proline--tRNA ligase, proS:prolyl-tRNA synthetase] [GN:proS][CL:proline--tRNA ligase] [OR:Bacillus subtilis] [EC:6.1.1.15] 153SPX1427 1427 4088 336 1008 691 5.20E-109 [LN:G69682] [AC:G69682][PN:proline--tRNA ligase, proS:prolyl-tRNA synthetase] [GN:proS][CL:proline--tRNA ligase] [OR:Bacillus subtilis] [EC:6.1.1.15] 153SPX1428 1428 4089 420 1260 436 8.50E-136 [GI:5714510] [LN:AF152237][AC:AF152237] [PN:Eep] [GN:eep] [FN:determinant for enhanced expressionof] [OR:Enterococcus faecalis] 129 SPX1429 1429 4090 268 804 2021.20E-51 [LN:CDSA_BACSU] [AC:O31752] [GN:CDSA] [OR:Bacillus subtilis][EC:2.7.7.41] [DE:SYNTHASE)] [SP:O31752] 101 SPX1430 1430 4091 259 777490 2.80E-90 [LN:UPPS_BACSU] [AC:O31751] [GN:UPPS] [OR:Bacillussubtilis] [EC:2.5.1.31][DE:(DI-TRANS-POLY-CIS-DECAPRENYLCISTRANSFERASE)] [SP:O31751] 136SPX1431 1431 4092 191 573 127 1.50E-11 [LN:S70841] [AC:S70841][PN:hypothetical transmembrane protein (sipS 3′region)][CL:Bradyrhizobium japonicum hypothetical transmembrane protein (sipS3′region)] [OR:Bradyrhizobium japonicum] 192 SPX1432 1432 4093 333 9991045 1.50E-140 [LN:H81105] [AC:H81105] [PN:Holliday junction DNAhelicase RuvB NMB1243 [imported]] [GN:NMB1243] [OR:Neisseriameningitidis] 124 SPX1433 1433 4094 35 105 76 0.00015 [LN:H72613][AC:H72613] [PN:hypothetical protein APE1371] [GN:APE1371] [OR:Aeropyrumpernix] 92 SPX1434 1434 4095 139 417 103 1.50E-06 [GI:5616248][LN:AF158628] [AC:AF158628] [PN:hypothetical protein][OR:Prochlorococcus PCC9511] 95 SPX1435 1435 4096 232 696 482 1.50E-73[LN:YIW2_YEAST] [AC:P40586] [GN:YIR042C] [OR:Saccharomyces cerevisiae][SR:,Baker′s yeast] [DE:HYPOTHETICAL 27.4 KD PROTEIN IN HYR1 3′REGION][SP:P40586] 155 SPX1436 1436 4097 64 192 NO-HIT 6 SPX1437 1437 4098 8342502 944 0 LN:C70131] [AC:C70131] [PN:leucine--tRNA ligase,leuS:leucyl-tRNA synthetase:leucyl-tRNA synthetase] [CL:leucine--tRNAligase] [OR:Borrelia burgdorferi] [SR:, Lyme disease spirochete][EC:6.1.1.4] 199 SPX1438 1438 4099 363 1089 998 1.00E-137[LN:GLDA_BACST] [AC:P32816] [GN:GLDA:GLD] [OR:Bacillusstearothermophilus] [EC:1.1.1.6] [DE:GLYCEROL DEHYDROGENASE, (GLDH)][SP:P32816] 137 SPX1439 1439 4100 223 669 356 8.20E-53 [GI:2582658][LN:CBAJ2527] [AC:AJ002527] [PN:OrfX] [GN:orfX] [FN:putativetransaldolase (37.4% identity to talC] [OR:Clostridium beijerinckii] 142SPX1440 1440 4101 816 2448 992 1.80E-275 [LN:PFLF_ECOLI] [AC:P75793][GN:YBIW] [OR:Escherichia coli] [EC:2.3.1.54] [DE:LYASE 3)] [SP:P75793]99 SPX1441 1441 4102 427 1281 337 4.90E-89 [LN:PTCC_BACST] [AC:Q45400][GN:CELB] [OR:Bacillus stearothermophilus] [DE:PERMEASE IIC COMPONENT)(PHOSPHOTRANSFERASE ENZYME II, C COMPONENT)] [SP:Q45400] 157 SPX14421442 4103 103 309 194 3.50E-22 [LN:A69785] [AC:A69785] [PN:cellobiosephosphotransferase system enzym homolog ydhM] [GN:ydhM][CL:phosphotransferase system enzyme II cellobiose-specific factor IIB][OR:Bacillus subtilis] 189 SPX1443 1443 4104 107 321 186 5.70E-21[LN:PTCA_BACSU] [AC:P46319] [GN:CELC:LICA] [OR:Bacillus subtilis][EC:2.7.1.69] [DE:(EC 2.7.1.69) (EIII-CEL)] [SP:P46319] 121 SPX1444 14444105 327 981 265 2.80E-49 [LN:SORC_KLEPN] [AC:P37078] [GN:SORC][OR:Klebsiella pneumoniae] [DE:SORBITOL OPERON REGULATOR (SOR OPERONACTIVATOR)] [SP:P37078] 130 SPX1445 1445 4106 249 747 252 6.10E-57[LN:YCIT_ECOLI] [AC:P76034] [GN:YCIT] [OR:Escherichia coli][DE:HYPOTHETICAL TRANSCRIPTIONAL REGULATOR IN OSMB-RNB INTERGENICREGION] [SP:P76034] 145 SPX1446 1446 4107 259 777 266 4.40E-55[LN:PFLE_ECOLI] [AC:P75794] [GN:YBIY] [OR:Escherichia coli][EC:1.97.1.4] [DE:PUTATIVE PYRUVATE FORMATE-LYASE 3 ACTIVATING ENZYME,][SP:P75794] 145 SPX1447 1447 4108 83 249 105 3.60E-08 [GI:7331182][LN:AF235048] [AC:AF235048] [PN:AgpT] [GN:agpT] [OR:Sinorhizobiummeliloti] 88 SPX1448 1448 4109 65 195 177 4.60E-18 [GI:6127225][LN:SHU75349] [AC:U75349] [PN:periplasmic-iron-binding protein BitA][GN:bit operon] [OR:Brachyspira hyodysenteriae] 129 SPX1449 1449 4110123 369 242 1.10E-26 [GI:6127225] [LN:SHU75349] [AC:U75349][PN:periplasmic-iron-binding protein BitA] [GN:bit operon][OR:Brachyspira hyodysenteriae] 129 SPX1450 1450 4111 318 954 7991.70E-113 [GI:2766194] [LN:SHU75349] [AC:U75349] [PN:putative ABCtransporter BitD] [GN:bit operon] [OR:Brachyspira hyodysenteriae] 121SPX1451 1451 4112 209 627 283 2.70E-40 [GI:2766195] [LN:SHU75349][AC:U75349] [PN:putative permease BitE] [GN:bit operon] [OR:Brachyspirahyodysenteriae] 114 SPX1452 1452 4113 257 771 295 1.50E-68 [GI:2766196][LN:SHU75349] [AC:U75349] [PN:putative permease BitF] [GN:bit operon][OR:Brachyspira hyodysenteriae] 114 SPX1453 1453 4114 66 198 1643.20E-17 [GI:2766196] [LN:SHU75349] [AC:U75349] [PN:putative permeaseBitF] [GN:bit operon] [OR:Brachyspira hyodysenteriae] 114 SPX1454 14544115 250 750 137 3.20E-10 [LN:PMGY_TREPA] [AC:P96121][GN:GPM:PGM:TP0168] [OR:Treponema pallidum] [EC:5.4.2.1][DE:(BPG-DEPENDENT PGAM)] [SP:P96121] 122 SPX1455 1455 4116 446 1338 8556.60E-196 [GI:7380543] [LN:NMA6Z2491] [AC:AL162757:AL157959][PN:conserved hypothetical protein] [GN:NMA1908] [OR:Neisseriameningitidis] 127 SPX1456 1456 4117 120 360 123 9.30E-21 [LN:E64494][AC:E64494] [PN:hypothetical protein MJ1558] [OR:Methanococcusjannaschii] 86 SPX1457 1457 4118 129 387 282 2.20E-58 [LN:T44411][AC:T44411] [PN:ribosomal protein L17 [imported]] [GN:rplQ][CL:Escherichia coli ribosomal protein L17] [OR:Bacillus halodurans] 140SPX1458 1458 4119 312 936 963 6.70E-130 [LN:RPOA_BACSU] [AC:P20429][GN:RPOA] [OR:Bacillus subtilis] [EC:2.7.7.6] [DE:ALPHA CHAIN) (RNAPOLYMERASE ALPHA SUBUNIT)] [SP:P20429] 134 SPX1459 1459 4120 134 402NO-HIT 6 SPX1460 1460 4121 141 423 494 1.80E-63 [LN:RS11_BACSU][AC:P04969] [GN:RPSK] [OR:Bacillus subtilis] [DE:30S RIBOSOMAL PROTEINS11 (BS11)] [SP:P04969] 110 SPX1461 1461 4122 122 366 433 1.70E-55[GI:1044989] [LN:BACRPLP] [AC:L47971] [PN:ribosomal protein S13][GN:rpsM] [OR:Bacillus subtilis] 97 SPX1462 1462 4123 56 168 2371.10E-28 [LN:S17988] [AC:S17988] [PN:translation initiation factor IF-1][GN:infA] [CL:translation initiation factor IF-1] [OR:Lactococcus lactissubsp. lactis] 151 SPX1463 1463 4124 213 639 560 8.10E-95 [LN:KAD_LACLA][AC:P27143] [GN:ADK] [OR:Lactococcus lactis][SR:,subsplactis:Streptococcus lactis] [EC:2.7.4.3] [DE:ADENYLATEKINASE, (ATP-AMP TRANSPHOSPHORYLASE)] [SP:P27143] 177 SPX1464 1464 4125437 1311 927 4.30E-126 [LN:SECY_LACLA] [AC:P27148] [GN:SECY][OR:Lactococcus lactis] [SR:,subsplactis:Streptococcus lactis][DE:PREPROTEIN TRANSLOCASE SECY SUBUNIT] [SP:P27148] 155 SPX1465 14654126 147 441 614 7.90E-79 [LN:RL15_STAAU] [AC:O06445] [GN:RPLO][OR:Staphylococcus aureus] [DE:50S RIBOSOMAL PROTEIN L15] [SP:O06445]107 SPX1466 1466 4127 61 183 185 6.90E-21 [LN:RL30_STAAU] [AC:O06444][GN:RPMD] [OR:Staphylococcus aureus] [DE:50S RIBOSOMAL PROTEIN L30][SP:O06444] 107 SPX1467 1467 4128 165 495 621 8.70E-81 [LN:RS5_BACST][AC:P02357] [GN:RPSE] [OR:Bacillus stearothermophilus] [DE:30S RIBOSOMALPROTEIN S5 (BS5)] [SP:P02357] 117 SPX1468 1468 4129 119 357 232 2.60E-53[LN:RL18_BACSU] [AC:P46899:P70969] [GN:RPLR] [OR:Bacillus subtilis][DE:50S RIBOSOMAL PROTEIN L18] [SP:P46899:P70969] 117 SPX1469 1469 4130175 525 478 2.00E-66 [LN:B69695] [AC:B69695] [PN:ribosomal protein L6(BL8) rplF] [GN:rplF] [CL:Escherichia coli ribosomal protein L6][OR:Bacillus subtilis] 136 SPX1470 1470 4131 133 399 521 2.60E-67[GI:1044978] [LN:BACRPLP] [AC:L47971] [PN:ribosomal protein S8][GN:rpsH] [OR:Bacillus subtilis] 96 SPX1471 1471 4132 79 237 NO-HIT 6SPX1472 1472 4133 90 270 325 8.80E-41 [LN:F69835] [AC:F69835][PN:ribosomal protein S14 homolog yhzA] [GN:yhzA] [CL:Escherichia coliribosomal protein S14] [OR:Bacillus subtilis] 140 SPX1473 1473 4134 181543 728 6.40E-96 [LN:T44395] [AC:T44395] [PN:ribosomal protein L5[imported]] [GN:rplE] [CL:Escherichia coli ribosomal protein L5][OR:Bacillus halodurans] 138 SPX1474 1474 4135 102 306 508 2.80E-65[GI:4927751] [LN:AF126059] [AC:AF126059] [PN:RpL24] [GN:rplX][OR:Streptococcus pneumoniae] 91 SPX1475 1475 4136 123 369 597 2.20E-78[GI:4927750] [LN:AF126059] [AC:AF126059] [PN:RpL14] [GN:rplN][OR:Streptococcus pneumoniae] 91 SPX1476 1476 4137 110 330 100 4.40E-07[LN:E71186] [AC:E71186] [PN:hypothetical protein PH1769] [GN:PH1769][CL:Pyrococcus horikoshii hypothetical protein PH1769] [OR:Pyrococcushorikoshii] 150 SPX1477 1477 4138 87 261 430 3.10E-55 [GI:4927749][LN:AF126059] [AC:AF126059] [PN:RpS17] [GN:rpsQ] [OR:Streptococcuspneumoniae] 91 SPX1478 1478 4139 133 399 NO-HIT 6 SPX1479 1479 4140 69207 324 8.90E-40 [GI:4927748] [LN:AF126059] [AC:AF126059] [PN:RpL29][GN:rpmC] [OR:Streptococcus pneumoniae] 91 SPX1480 1480 4141 138 414 7081.30E-94 [GI:4927747] [LN:AF126059] [AC:AF126059] [PN:RpL16] [GN:rplP][OR:Streptococcus pneumoniae] 91 SPX1481 1481 4142 209 627 10632.10E-142 [GI:4927746] [LN:AF126059] [AC:AF126059] [PN:RpS3] [GN:rpsC][OR:Streptococcus pneumoniae] 90 SPX1482 1482 4143 75 225 356 1.60E-44[GI:4927745] [LN:AF126059] [AC:AF126059] [PN:RpL22] [GN:rplV][OR:Streptococcus pneumoniae] 91 SPX1483 1483 4144 82 246 NO-HIT 6SPX1484 1484 4145 94 282 492 5.20E-64 [GI:4927744] [LN:AF126059][AC:AF126059] [PN:RpS19] [GN:rpsS] [OR:Streptococcus pneumoniae] 91SPX1485 1485 4146 278 834 1144 2.80E-152 [LN:RL2_BACST] [AC:P04257][GN:RPLB] [OR:Bacillus stearothermophilus] [DE:50S RIBOSOMAL PROTEIN L2][SP:P04257] 111 SPX1486 1486 4147 99 297 162 1.30E-30 [GI:3273331][LN:AB015722] [AC:AB015722] [PN:ribosomal protrein L23] [OR:Bacillusstearothermophilus] [SR:Bacillus stearothermophilus DNA] 138 SPX14871487 4148 208 624 696 6.80E-91 [LN:RL4_BACST] [AC:P28601] [GN:RPLD][OR:Bacillus stearothermophilus] [DE:50S RIBOSOMAL PROTEIN L4][SP:P28601] 111 SPX1488 1488 4149 209 627 496 6.60E-110 [LN:RL3_BACSU][AC:P42920] [GN:RPLC] [OR:Bacillus subtilis] [DE:50S RIBOSOMAL PROTEINL3 (BL3)] [SP:P42920] 107 SPX1489 1489 4150 103 309 494 3.40E-64[LN:RS10_STRMU] [AC:P48853] [GN:RPSJ] [OR:Streptococcus mutans] [DE:30SRIBOSOMAL PROTEIN S10] [SP:P48853] 106 SPX1490 1490 4151 206 618 710.00018 [GI:7302797] [LN:AE003803] [AC:AE003803:AE002787] [GN:CG4798][OR:Drosophila melanogaster] [SR:fruit fly] 105 SPX1491 1491 4152 197591 843 3.60E-112 [GI:4098082] [LN:LLU73336] [AC:U73336] [PN:anaerobicribonucleotide reductase activator] [GN:nrdG] [FN:activation ofanaerobic] [OR:Lactococcus lactis subsp. cremoris] 167 SPX1492 1492 415369 207 NO-HIT 6 SPX1493 1493 4154 169 507 187 4.50E-19 [LN:G75479][AC:G75479] [PN:hypothetical protein] [GN:DR0763] [OR:Deinococcusradiodurans] 90 SPX1494 1494 4155 155 465 NO-HIT 6 SPX1495 1495 4156 7382214 1123 1.10E-231 [GI:4098081] [LN:LLU73336] [AC:U73336] [PN:anaerobicribonucleotide reductase] [GN:nrdD] [OR:Lactococcus lactis subsp.cremoris] 128 SPX1496 1496 4157 519 1557 NO-HIT 6 SPX1497 1497 4158 4921476 519 3.70E-97 [LN:YWAP_STRMU] [AC:P34001] [OR:Streptococcus mutans][DE:HYPOTHETICAL PROTEIN IN WAPA 3′REGION (FRAGMENT)] [SP:P34001] 119SPX1498 1498 4159 186 558 93 0.00012 [LN:A26892] [AC:A26892] [PN:Mopabox protein] [OR:Mus musculus] [SR:, house mouse] 84 SPX1499 1499 416070 210 NO-HIT 6 SPX1500 1500 4161 130 390 66 7.30E-09 [GI:1119198][LN:BACCOMC] [AC:M30805] [PN:unknown protein] [OR:Bacillus subtilis][SR:Bacillus subtilis (strain IS75) DNA] 122 SPX1501 1501 4162 161 483119 5.10E-16 [LN:FOLC_LACCA] [AC:P15925] [GN:FGS] [OR:Lactobacilluscasei] [EC:6.3.2.17] [DE:SYNTHETASE) (FPGS)] [SP:P15925] 111 SPX15021502 4163 164 492 251 2.00E-38 [LN:FOLC_BACSU] [AC:Q05865] [GN:FOLC][OR:Bacillus subtilis] [EC:6.3.2.17] [DE:SYNTHETASE) (FPGS)] [SP:Q05865]110 SPX1503 1503 4164 102 306 87 5.90E-11 [LN:A69982] [AC:A69982][PN:hypothetical protein yrzB] [GN:yrzB] [OR:Bacillus subtilis] 87SPX1504 1504 4165 140 420 327 2.00E-40 [LN:D69979] [AC:D69979][PN:conserved hypothetical protein yrrK] [GN:yrrK] [CL:Haemophilusinfluenzae conserved hypothetical protein HI0305] [OR:Bacillus subtilis]163 SPX1505 1505 4166 89 267 NO-HIT 6 SPX1506 1506 4167 190 570 NO-HIT 6SPX1507 1507 4168 133 399 315 1.80E-38 [GI:6650536] [LN:AF103794][AC:AF103794] [PN:unknown] [OR:Listeria monocytogenes] 81 SPX1508 15084169 126 378 333 1.60E-40 [GI:517210] [LN:SPU11799] [AC:U11799][OR:Streptococcus pyogenes] 65 SPX1509 1509 4170 131 393 340 3.70E-41[GI:517210] [LN:SPU11799] [AC:U11799] [OR:Streptococcus pyogenes] 65SPX1510 1510 4171 296 888 1035 8.50E-139 [GI:6318592] [LN:AF146529][AC:AF146529] [PN:aromatic amino acid aminotransferase] [GN:araT][FN:catalyzes the last reaction in the biosynthesis] [OR:Lactococcuslactis subsp. cremoris] 185 SPX1511 1511 4172 62 186 NO-HIT 6 SPX15121512 4173 257 771 297 2.20E-40 [LN:YQXN_BACSU] [AC:P42095][GN:YQXN:YQFI] [OR:Bacillus subtilis] [DE:(ORF3)] [SP:P42095] 89 SPX15131513 4174 331 993 623 6.80E-120 [LN:H69679] [AC:H69679] [PN:involved infatty acid/phospholipid synthesis plsX] [GN:plsX] [CL:phospholipidsynthesis protein] [OR:Bacillus subtilis] 148 SPX1514 1514 4175 112 336NO-HIT 6 SPX1515 1515 4176 78 234 129 1.40E-17 [LN:C72349] [AC:C72349][PN:acyl carrier protein] [GN:TM0662] [CL:acyl carrier protein:acylcarrier protein homology] [OR:Thermotoga maritima] 142 SPX1516 1516 417798 294 320 4.80E-40 [LN:S52544] [AC:S52544] [PN:ISL2 protein][OR:Lactobacillus helveticus] 71 SPX1517 1517 4178 77 231 64 3.00E-06[GI:2695624] [LN:STU93029] [AC:U93029] [PN:amphipathic pore-formingpeptide precursor] [GN:thmA] [OR:Streptococcus thermophilus] 128 SPX15181518 4179 69 207 NO-HIT 6 SPX1519 1519 4180 720 2160 3571 0[LN:COMA_STRPN] [AC:Q03727] [GN:COMA] [OR:Streptococcus pneumoniae][DE:TRANSPORT ATP-BINDING PROTEIN COMA] [SP:Q03727] 119 SPX1520 15204181 450 1350 2184 8.20E-289 [LN:COMB_STRPN] [AC:P36498] [GN:COMB][OR:Streptococcus pneumoniae] [DE:TRANSPORT PROTEIN COMB] [SP:P36498]107 SPX1521 1521 4182 250 750 1189 1.40E-160 [LN:PUR7_STRPN] [AC:Q07296][GN:PURC] [OR:Streptococcus pneumoniae] [EC:6.3.2.6] [DE:(SAICARSYNTHETASE)] [SP:Q07296] 117 SPX1522 1522 4183 254 762 127 2.80E-08[LN:C69492] [AC:C69492] [PN:phosphoribosylformylglycinamidine synthase,component II:formylglycinamide ribotideamidotransferase:phosphoribosylformylglycinamidine synthetase][OR:Archaeoglobus fulgidus] [EC:6.3.5.3] 217 SPX1523 1523 4184 95 285155 3.80E-15 [GI:4928281] [LN:AF132127] [AC:AF132127][PN:glucose-6-phosphate isomerase] [GN:gpi] [OR:Streptococcus mutans]110 SPX1524 1524 4185 457 1371 1764 1.20E-238 [GI:4928281] [LN:AF132127][AC:AF132127] [PN:glucose-6-phosphate isomerase] [GN:gpi][OR:Streptococcus mutans] 110 SPX1525 1525 4186 246 738 246 3.10E-28[LN:YDP3_LACLA] [AC:P22347] [OR:Lactococcus lactis][SR:,subsplactis:Streptococcus lactis] [DE:HYPOTHETICAL 18.7 KD PROTEININ PEPX 3′REGION (ORF3)] [SP:P22347] 162 SPX1526 1526 4187 604 1812 10012.10E-222 [GI:4104142] [LN:AF033015] [AC:AF033015] [PN:ABC transporterhomolog Z] [OR:Listeria monocytogenes] 99 SPX1527 1527 4188 72 216NO-HIT 6 SPX1528 1528 4189 108 324 105 1.60E-07 [GI:6015958][LN:SSU18930] [AC:Y18930] [PN:hypothetical protein] [GN:ORF-c22_037][OR:Sulfolobus solfataricus] 110 SPX1529 1529 4190 196 588 455 7.30E-58[GI:4104141] [LN:AF033015] [AC:AF033015] [PN:ABC transporter homolog Y][OR:Listeria monocytogenes] 99 SPX1530 1530 4191 361 1083 422 2.80E-66[GI:4104140] [LN:AF033015] [AC:AF033015] [PN:ABC transporter homolog X][OR:Listeria monocytogenes] 99 SPX1531 1531 4192 655 1965 3290 0[LN:HEXA_STRPN] [AC:P10564] [GN:HEXA] [OR:Streptococcus pneumoniae][DE:DNA MISMATCH REPAIR PROTEIN HEXA] [SP:P10564] 117 SPX1532 1532 4193182 546 859 6.40E-114 [LN:HEXA_STRPN] [AC:P10564] [GN:HEXA][OR:Streptococcus pneumoniae] [DE:DNA MISMATCH REPAIR PROTEIN HEXA][SP:P10564] 117 SPX1533 1533 4194 149 447 740 7.50E-99 [LN:ARGR_STRPN][AC:Q54870] [GN:ARGR] [OR:Streptococcus pneumoniae] [DE:PROBABLEARGININE REPRESSOR] [SP:Q54870] 112 SPX1534 1534 4195 564 1692 3653.20E-102 [LN:SYRC_YEAST] [AC:Q05506] [GN:YDR341C:D9651.10][OR:Saccharomyces cerevisiae] [SR:,Baker′s yeast] [EC:6.1.1.19][DE:-TRNA LIGASE) (ARGRS)] [SP:Q05506] 154 SPX1535 1535 4196 150 450 3986.20E-51 [LN:S52544] [AC:S52544] [PN:ISL2 protein] [OR:Lactobacillushelveticus] 71 SPX1536 1536 4197 68 204 NO-HIT 6 SPX1537 1537 4198 95285 102 6.20E-17 [LN:S74709] [AC:S74709] [PN:hypothetical proteinsll1188] [OR:Synechocystis sp.] [SR:PCC 6803, , PCC 6803] [SR:PCC 6803,] 124 SPX1538 1538 4199 236 708 1209 4.90E-164 [GI:5830529][LN:SPAJ6394] [AC:AJ006394] [PN:response regulator] [GN:phoP][OR:Streptococcus pneumoniae] 104 SPX1539 1539 4200 444 1332 21964.10E-300 [GI:5830530] [LN:SPAJ6394] [AC:AJ006394] [PN:histidine kinase][GN:phoR] [OR:Streptococcus pneumoniae] 102 SPX1540 1540 4201 292 8761435 1.70E-188 [GI:4530447] [LN:AF118229] [AC:AF118229] [PN:phosphatebinding protein PstS] [GN:pstS] [OR:Streptococcus pneumoniae] 116SPX1541 1541 4202 272 816 1333 2.80E-185 [GI:4530448] [LN:AF118229][AC:AF118229] [PN:transmembrane protein PstC] [GN:pstC][OR:Streptococcus pneumoniae] 112 SPX1542 1542 4203 272 816 13121.10E-182 [GI:4530449] [LN:AF118229] [AC:AF118229] [PN:transmembraneprotein PstA] [GN:PstA] [OR:Streptococcus pneumoniae] 112 SPX1543 15434204 251 753 1284 2.00E-174 [GI:4530450] [LN:AF118229] [AC:AF118229][PN:ATP-binding cassette protein PstB] [GN:pstB] [OR:Streptococcuspneumoniae] 119 SPX1544 1544 4205 217 651 1067 8.20E-144 [GI:4530451][LN:AF118229] [AC:AF118229] [PN:PhoU] [GN:phoU] [OR:Streptococcuspneumoniae] 90 SPX1545 1545 4206 142 426 131 2.90E-10 [GI:5822769][LN:AB024553] [AC:AB024553] [OR:Bacillus halodurans] [SR:Bacillushalodurans (strain:C-125) DNA] 109 SPX1546 1546 4207 73 219 NO-HIT 6SPX1547 1547 4208 153 459 NO-HIT 6 SPX1548 1548 4209 339 1017 9216.40E-122 [LN:GPDA_BACSU] [AC:P46919] [GN:GPSA:GLYC] [OR:Bacillussubtilis] [EC:1.1.1.94] [DE:DEPENDENT DIHYDROXYACETONE-PHOSPHATEREDUCTASE)] [SP:P46919] 144 SPX1549 1549 4210 300 900 1481 1.60E-199[GI:3550619] [LN:SPAJ4869] [AC:AJ004869] [PN:UTP-glucose-1-phosphateuridylyltransferase] [GN:galU] [FN:synthesis of UDP-glucose][OR:Streptococcus pneumoniae] 159 SPX1550 1550 4211 225 675 NO-HIT 6SPX1551 1551 4212 227 681 520 1.90E-70 [LN:SUB400707] [AC:AJ400707][PN:hypothetical protein] [OR:Streptococcus uberis] 80 SPX1552 1552 4213182 546 236 1.30E-55 [GI:3192049] [LN:AB001562] [AC:AB001562][OR:Streptococcus mutans] [SR:Streptococcus mutans (strain:Xc) DNA] 108SPX1553 1553 4214 377 1131 622 4.50E-119 [LN:G69866] [AC:G69866][PN:hippurate hydrolase homolog ykuR] [GN:ykuR] [CL:hippurate hydrolase][OR:Bacillus subtilis] 119 SPX1554 1554 4215 233 699 578 1.10E-86[LN:H72245] [AC:H72245] [PN:2,3,4,5-tetrahydropyridine-2-carboxylateN-succinyltransferase-related protein] [GN:TM1519] [OR:Thermotogamaritima] 146 SPX1555 1555 4216 153 459 75 5.50E-08 [GI:6103625][LN:AF172095] [AC:AF172095] [PN:unknown] [OR:Picea rubens] 71 SPX15561556 4217 72 216 NO-HIT 6 SPX1557 1557 4218 278 834 214 2.60E-30[LN:YDED_BACSU] [AC:P96661] [GN:YDED] [OR:Bacillus subtilis][DE:HYPOTHETICAL 35.3 KD PROTEIN IN CSPC-NAP INTERGENIC REGION][SP:P96661] 136 SPX1558 1558 4219 821 2463 4147 0 [GI:6165962][LN:AF101781] [AC:AF101781] [PN:penicillin-binding protein 1b][GN:pbp1b] [OR:Streptococcus pneumoniae] 116 SPX1559 1559 4220 419 1257697 1.90E-174 [LN:SYY1_BACSU] [AC:P22326] [GN:TYRS] [OR:Bacillussubtilis] [EC:6.1.1.1] [DE:(TYRRS 1)] [SP:P22326] 100 SPX1560 1560 4221691 2073 218 1.60E-63 [LN:COPA_ENTHR] [AC:P32113:Q47841] [GN:COPA][OR:Enterococcus hirae] [EC:3.6.1.36] [DE:COPPER/POTASSIUM-TRANSPORTINGATPASE A,] [SP:P32113:Q47841] 148 SPX1561 1561 4222 65 195 NO-HIT 6SPX1562 1562 4223 88 264 109 2.90E-08 [LN:RRMA_ECOLI] [AC:P36999][GN:RRMA] [OR:Escherichia coli] [EC:2.1.1.51] [DE:METHYLTRANSFERASE)][SP:P36999] 109 SPX1563 1563 4224 197 591 192 1.90E-25 [LN:YXJB_BACSU][AC:P42313] [GN:YXJB:N15I] [OR:Bacillus subtilis] [DE:HYPOTHETICAL 31.5KD PROTEIN IN KATB 3′REGION] [SP:P42313] 128 SPX1564 1564 4225 57 171NO-HIT 6 SPX1565 1565 4226 191 573 NO-HIT 6 SPX1566 1566 4227 753 2259473 5.80E-165 [LN:PHSG_BACSU] [AC:P39123] [GN:GLGP] [OR:Bacillussubtilis] [EC:2.4.1.1] [DE:GLYCOGEN PHOSPHORYLASE,] [SP:P39123] 116SPX1567 1567 4228 506 1518 2687 0 [LN:MALQ_STRPN] [AC:P29851] [GN:MALM][OR:Streptococcus pneumoniae] [EC:2.4.1.25] [DE:(DISPROPORTIONATINGENZYME) (D-ENZYME)] [SP:P29851] 137 SPX1568 1568 4229 424 1272 21673.30E-288 [LN:MALX_STRPN] [AC:P29850] [GN:MALX] [OR:Streptococcuspneumoniae] [DE:MALTOSE/MALTODEXTRIN-BINDING PROTEIN PRECURSOR][SP:P29850] 131 SPX1569 1569 4230 431 1293 2176 0 [LN:MALC_STRPN][AC:Q04698] [GN:MALC] [OR:Streptococcus pneumoniae] [DE:MALTODEXTRINTRANSPORT SYSTEM PERMEASE PROTEIN MALC] [SP:Q04698] 136 SPX1570 15704231 281 843 1265 2.40E-177 [LN:MALD_STRPN] [AC:Q04699] [GN:MALD][OR:Streptococcus pneumoniae] [DE:MALTODEXTRIN TRANSPORT SYSTEM PERMEASEPROTEIN MALD] [SP:Q04699] 136 SPX1571 1571 4232 267 801 540 1.70E-145[LN:MALA_STRPN] [AC:Q08510] [GN:MALA] [OR:Streptococcus pneumoniae][DE:MALA PROTEIN] [SP:Q08510] 97 SPX1572 1572 4233 329 987 16687.30E-227 [GI:2656094] [LN:STRMALR] [AC:L21856] [PN:repressor protein][GN:malR] [FN:maltose operon transcriptional repressor][OR:Streptococcus pneumoniae] 146 SPX1573 1573 4234 114 342 NO-HIT 6SPX1574 1574 4235 127 381 378 8.30E-48 [LN:T30285] [AC:T30285][PN:hypothetical protein] [OR:Streptococcus pneumoniae] 79 SPX1575 15754236 314 942 463 6.90E-73 [GI:1620924] [LN:BS168NPRB] [AC:Z79580][OR:Bacillus subtilis] 62 SPX1576 1576 4237 588 1764 701 1.30E-229[LN:SYD_BACSU] [AC:O32038] [GN:ASPS] [OR:Bacillus subtilis][EC:6.1.1.12] [DE:(ASPRS)] [SP:O32038] 98 SPX1577 1577 4238 144 432NO-HIT 6 SPX1578 1578 4239 64 192 NO-HIT 6 SPX1579 1579 4240 77 231NO-HIT 6 SPX1580 1580 4241 214 642 120 9.80E-14 [GI:1402529] [LN:D78257][AC:D78257] [PN:ORF8] [GN:orf8] [OR:Enterococcus faecalis][SR:Enterococcus faecalis plasmid:pYI17 DNA] 128 SPX1581 1581 4242 247741 NO-HIT 6 SPX1582 1582 4243 67 201 NO-HIT 6 SPX1583 1583 4244 155 46578 0.00011 [LN:T07291] [AC:T07291] [PN:hypothetical protein 42c][OR:chloroplast Chlorella vulgaris] 89 SPX1584 1584 4245 62 186 NO-HIT 6SPX1585 1585 4246 64 192 NO-HIT 6 SPX1586 1586 4247 63 189 200 7.00E-24[LN:T30285] [AC:T30285] [PN:hypothetical protein] [OR:Streptococcuspneumoniae] 79 SPX1587 1587 4248 430 1290 1740 7.50E-236 [LN:SYH_STREQ][AC:P30053] [GN:HISS] [OR:Streptococcus equisimilis] [EC:6.1.1.21][DE:(HISRS)] [SP:P30053] 106 SPX1588 1588 4249 307 921 NO-HIT 6 SPX15891589 4250 416 1248 334 2.10E-57 [GI:3582221] [LN:AE001272] [AC:AE001272][PN:conserved hypothetical protein] [GN:ORF00049] [OR:Lactococcuslactis] 114 SPX1590 1590 4251 133 399 NO-HIT 6 SPX1591 1591 4252 284 852301 1.70E-34 [LN:RGG_STRGC] [AC:P49330] [GN:RGG] [OR:Streptococcusgordonii challis] [DE:RGG PROTEIN] [SP:P49330] 100 SPX1592 1592 4253 114342 227 6.60E-27 [GI:2258088] [LN:AB000631] [AC:AB000631][OR:Streptococcus mutans] [SR:Streptococcus mutans DNA] 96 SPX1593 15934254 568 1704 994 1.30E-207 [LN:S76895] [AC:S76895] [PN:hypotheticalprotein] [CL:dihydroxy-acid dehydratase] [OR:Synechocystis sp.] [SR:PCC6803, , PCC 6803] [SR:PCC 6803, ] 148 SPX1594 1594 4255 311 933 2722.40E-45 [LN:TKTC_METJA] [AC:Q58092] [GN:MJ0679] [OR:Methanococcusjannaschii] [EC:2.2.1.1] [DE:PUTATIVE TRANSKETOLASE C-TERMINAL SECTION,(TK)] [SP:Q58092] 149 SPX1595 1595 4256 286 858 347 7.70E-66[LN:TKTN_METJA] [AC:Q58094] [GN:MJ0681] [OR:Methanococcus jannaschii][EC:2.2.1.1] [DE:PUTATIVE TRANSKETOLASE N-TERMINAL SECTION, (TK)][SP:Q58094] 149 SPX1596 1596 4257 449 1347 535 9.90E-132 [LN:T37066][AC:T37066] [PN:probable integral membrane protein] [GN:SCJ21.17c][OR:Streptomyces coelicolor] 107 SPX1597 1597 4258 95 285 NO-HIT 6SPX1598 1598 4259 677 2031 197 8.80E-31 [GI:4512373] [LN:AB011837][AC:AB011837] [GN:yjdC] [OR:Bacillus halodurans] [SR:Bacillus halodurans(strain:C-125) DNA, clone_lib:lambda no.9] 144 SPX1599 1599 4260 3361008 133 1.30E-18 [GI:6689167] [LN:SCE20] [AC:AL136058] [PN:putativemembrane protein] [GN:SCE20.08c] [OR:Streptomyces coelicolor A3(2)] 118SPX1600 1600 4261 67 201 NO-HIT 6 SPX1601 1601 4262 61 183 240 3.00E-28[LN:RL32_LACLC] [AC:O34101] [GN:RPMF] [OR:Lactococcus lactis][SR:,subspcremoris:Streptococcus cremoris] [DE:50S RIBOSOMAL PROTEINL32] [SP:O34101] 149 SPX1602 1602 4263 642 1926 1320 0 [GI:1914872][LN:SPZ82001] [AC:Z82001] [PN:PCPA] [GN:pcpA] [OR:Streptococcuspneumoniae] 88 SPX1603 1603 4264 76 228 NO-HIT 6 SPX1604 1604 4265 192576 429 4.10E-54 [LN:S52544] [AC:S52544] [PN:ISL2 protein][OR:Lactobacillus helveticus] 71 SPX1605 1605 4266 126 378 303 4.10E-37[LN:S52544] [AC:S52544] [PN:ISL2 protein] [OR:Lactobacillus helveticus]71 SPX1606 1606 4267 109 327 495 7.70E-65 [GI:1914871] [LN:SPZ82001][AC:Z82001] [PN:unknown] [OR:Streptococcus pneumoniae] 81 SPX1607 16074268 627 1881 95 0.00073 [LN:T27355] [AC:T27355] [PN:hypotheticalprotein Y70D2A.2] [GN:Y70D2A.2] [OR:Caenorhabditis elegans] 100 SPX16081608 4269 290 870 108 2.70E-22 [LN:F70203] [AC:F70203] [PN:xylose operonregulatory protein (xylR-2) homolog] [CL:glucose kinase:glucose kinasehomology] [OR:Borrelia burgdorferi] [SR:, Lyme disease spirochete] 181SPX1609 1609 4270 887 2661 345 6.30E-65 [LN:YBGG_ECOLI][AC:P54746:P75753] [GN:YBGG] [OR:Escherichia coli] [DE:HYPOTHETICAL100.0 KD PROTEIN IN HRSA-CYDA INTERGENIC REGION] [SP:P54746:P75753] 151SPX1610 1610 4271 435 1305 409 6.20E-106 [LN:T37125] [AC:T37125][PN:hypothetical protein SCJ4.42c] [GN:SCJ4.42c] [OR:Streptomycescoelicolor] 101 SPX1611 1611 4272 695 2085 408 9.50E-105 [GI:5759293][LN:AF175722] [AC:AF175722] [PN:immunoreactive 89kD antigen PG87][OR:Porphyromonas gingivalis] 108 SPX1612 1612 4273 560 1680 2492.20E-63 [GI:4096756] [LN:SSU39394] [AC:U39394][PN:alpha-1,3/4-fucosidase precursor] [FN:alpha-fucosidase specific foralpha-1,3 and] [OR:Streptomyces sp.] [SR:Streptomyces sp] 170 SPX16131613 4274 410 1230 942 1.30E-244 [LN:SAGP_STRPY] [AC:P16962] [GN:SAGP][OR:Streptococcus pyogenes] [DE:STREPTOCOCCAL ACID GLYCOPROTEIN][SP:P16962] 114 SPX1614 1614 4275 339 1017 897 3.80E-184 [GI:2764612][LN:LSAJ1330] [AC:AJ001330] [PN:ornithine transcarbamoylase] [GN:arcB][OR:Lactobacillus sakei] 108 SPX1615 1615 4276 316 948 465 3.40E-129[GI:2894540] [LN:EFAJ3331] [AC:AJ223331] [PN:carbamate kinase] [GN:arcC][FN:synthesis of ATP from carbamylphosphate] [OR:Enterococcus faecium]143 SPX1616 1616 4277 504 1512 426 4.50E-106 [GI:2697115] [LN:AF008219][AC:AF008219] [PN:unknown] [OR:Borrelia afzelii] 75 SPX1617 1617 4278444 1332 277 8.20E-67 [LN:S43914] [AC:S43914] [PN:hypothetical protein1] [CL:peptidase V] [OR:Bacillus stearothermophilus] 101 SPX1618 16184279 64 192 NO-HIT 6 SPX1619 1619 4280 79 237 NO-HIT 6 SPX1620 1620 428189 267 NO-HIT 6 SPX1621 1621 4282 51 153 NO-HIT 6 SPX1622 1622 4283 72216 176 4.20E-20 [LN:T30285] [AC:T30285] [PN:hypothetical protein][OR:Streptococcus pneumoniae] 79 SPX1623 1623 4284 55 165 NO-HIT 6SPX1624 1624 4285 300 900 560 2.70E-78 [GI:6714460] [LN:ATAC008261][AC:AC008261] [GN:T4P13.3] [OR:Arabidopsis thaliana] [SR:thale cress] 98SPX1625 1625 4286 64 192 NO-HIT 6 SPX1626 1626 4287 384 1152 8401.50E-119 [LN:ADH2_ECOLI] [AC:P37686] [GN:YIAY] [OR:Escherichia coli][EC:1.1.1.1] [DE:PROBABLE ALCOHOL DEHYDROGENASE,] [SP:P37686] 123SPX1627 1627 4288 589 1767 874 7.80E-287 [GI:6015981] [LN:AF137263][AC:AF137263] [PN:L-fucose isomerase] [GN:fucI] [OR:Bacteroidesthetaiotaomicron] 108 SPX1628 1628 4289 243 729 201 8.40E-20 [LN:B70645][AC:B70645] [PN:L-fuculose-phosphate aldolase,] [GN:fucA][CL:L-ribulose-phosphate 4-epimerase] [OR:Mycobacterium tuberculosis][EC:4.1.2.17] 155 SPX1629 1629 4290 1029 3087 NO-HIT 6 SPX1630 1630 4291738 2214 1709 3.00E-243 [GI:4567098] [LN:AF130985] [AC:AF130985][PN:alpha-galactosidase AgaN] [GN:agaN] [OR:Bacillus stearothermophilus]113 SPX1631 1631 4292 624 1872 112 5.60E-07 [LN:T36462] [AC:T36462][PN:hypothetical protein SCF85.02] [GN:SCF85.02] [OR:Streptomycescoelicolor] 101 SPX1632 1632 4293 440 1320 174 1.10E-50 [LN:T36467][AC:T36467] [PN:probable glycosyl hydrolase] [GN:SCF85.07][CL:alpha-L-fucosidase] [OR:Streptomyces coelicolor] 123 SPX1633 16334294 62 186 NO-HIT 6 SPX1634 1634 4295 295 885 372 3.60E-50[LN:YURM_BACSU] [AC:O32154] [GN:YURM] [OR:Bacillus subtilis][DE:HYPOTHETICAL ABC TRANSPORTER PERMEASE PROTEIN YURM] [SP:O32154] 128SPX1635 1635 4296 310 930 163 7.70E-27 [LN:E72357] [AC:E72357] [PN:sugarABC transporter, permease protein] [GN:TM0596] [CL:inner membraneprotein malF] [OR:Thermotoga maritima] 140 SPX1636 1636 4297 431 1293 845.60E-07 [GI:1524333] [LN:SCMALREFG] [AC:Y07706] [PN:putativemaltose-binding pootein] [GN:malE] [OR:Streptomyces coelicolor] 116SPX1637 1637 4298 468 1404 210 2.00E-81 [LN:E70014] [AC:E70014][PN:rhamnulokinase, yulC] [GN:yulC] [CL:rhamnulokinase] [OR:Bacillussubtilis] [EC:2.7.1.5] 117 SPX1638 1638 4299 59 177 NO-HIT 6 SPX16391639 4300 258 774 123 7.20E-21 [LN:SRLR_ECOLI] [AC:P15082:P77030][GN:SRLR:GUTR] [OR:Escherichia coli] [DE:GLUCITOL OPERON REPRESSOR][SP:P15082:P77030] 121 SPX1640 1640 4301 73 219 NO-HIT 6 SPX1641 16414302 69 207 NO-HIT 6 SPX1642 1642 4303 502 1506 2158 8.80E-289[LN:T46756] [AC:T46756] [PN:Zn-binding lipoprotein adcA [imported]][GN:adcA] [OR:Streptococcus pneumoniae] 107 SPX1643 1643 4304 269 8071261 4.10E-177 [LN:T46755] [AC:T46755] [PN:membrane protein adcB[imported]] [GN:adcB] [OR:Streptococcus pneumoniae] 101 SPX1644 16444305 235 705 1247 1.40E-168 [LN:T46754] [AC:T46754] [PN:AdcC protein[imported]] [GN:adcC] [OR:Streptococcus pneumoniae] 92 SPX1645 1645 430664 192 89 1.20E-06 [LN:G72536] [AC:G72536] [PN:hypothetical proteinAPE1580] [GN:APE1580] [OR:Aeropyrum pernix] 92 SPX1646 1646 4307 167 501728 1.10E-95 [LN:T46753] [AC:T46753] [PN:repressor protein adcR[imported]] [GN:adcR] [OR:Streptococcus pneumoniae] 102 SPX1647 16474308 428 1284 612 1.10E-162 [GI:3403204] [LN:AF050517][AC:AF050517:S78492] [PN:unknown] [GN:dlt4] [OR:Streptococcus mutans] 96SPX1648 1648 4309 80 240 360 8.20E-46 [GI:2981430] [LN:AF049357][AC:AF049357:S78492] [PN:Glg3] [GN:glg3] [OR:Streptococcus mutans] 93SPX1649 1649 4310 415 1245 1236 2.30E-227 [GI:2952530] [LN:AF051356][AC:AF051356] [PN:integral membrane protein] [GN:dltB] [OR:Streptococcusmutans] 107 SPX1650 1650 4311 517 1551 2154 1.90E-292 [LN:DLTA_STRMU][AC:Q53526:O68576] [GN:DLTA] [OR:Streptococcus mutans] [EC:6.3.2.-][DE:ALANYL CARRIER PROTEIN LIGASE) (DCL)] [SP:Q53526:O68576] 144 SPX16511651 4312 66 198 NO-HIT 6 SPX1652 1652 4313 174 522 215 3.50E-24[LN:H69812] [AC:H69812] [PN:conserved hypothetical protein yfmI][GN:yfmI] [OR:Bacillus subtilis] 97 SPX1653 1653 4314 237 711 972.60E-14 [LN:H69812] [AC:H69812] [PN:conserved hypothetical proteinyfmI] [GN:yfmI] [OR:Bacillus subtilis] 97 SPX1654 1654 4315 62 186NO-HIT 6 SPX1655 1655 4316 63 189 NO-HIT 6 SPX1656 1656 4317 331 9931712 2.40E-235 [GI:2804734] [LN:AF030367] [AC:AF030367][PN:maturase-related protein] [OR:Streptococcus pneumoniae] 100 SPX16571657 4318 94 282 470 6.40E-60 [GI:2804734] [LN:AF030367] [AC:AF030367][PN:maturase-related protein] [OR:Streptococcus pneumoniae] 100 SPX16581658 4319 82 246 NO-HIT 6 SPX1659 1659 4320 66 198 NO-HIT 6 SPX1660 16604321 196 588 NO-HIT 6 SPX1661 1661 4322 68 204 344 4.40E-42 [GI:1217989][LN:SPU12567] [AC:U12567] [PN:ORF3] [OR:Streptococcus pneumoniae] 78SPX1662 1662 4323 253 759 968 2.20E-159 [LN:GLPF_STRPN] [AC:P52281][GN:GLPF] [OR:Streptococcus pneumoniae] [DE:GLYCEROL UPTAKE FACILITATORPROTEIN] [SP:P52281] 120 SPX1663 1663 4324 609 1827 3058 0 [GI:3551774][LN:SPU94770] [AC:U94770] [PN:alpha-glycerophosphate oxidase] [GN:glpO][FN:oxidizes alpha-glycerophosphate to] [OR:Streptococcus pneumoniae]154 SPX1664 1664 4325 100 300 302 1.90E-38 [LN:S67936] [AC:S67936][PN:glycerol-3-phosphate dehydrogenase homolog GlpD] [GN:glpD][OR:Streptococcus pneumoniae] [SR:strain P13, , strain P13] [SR:strainP13, ] 166 SPX1665 1665 4326 503 1509 1251 2.90E-274 [LN:GLPK_ENTFA][AC:O34154] [GN:GLPK] [OR:Enterococcus faecalis] [SR:,Streptococcusfaecalis] [EC:2.7.1.30] [DE:(GLYCEROKINASE) (GK)] [SP:O34154] 147SPX1666 1666 4327 476 1428 NO-HIT 6 SPX1667 1667 4328 66 198 NO-HIT 6SPX1668 1668 4329 291 873 1063 2.60E-140 [GI:4033717] [LN:SPU49397][AC:U49397] [PN:unknown] [OR:Streptococcus pyogenes] 79 SPX1669 16694330 327 981 1303 4.70E-175 [GI:4033718] [LN:SPU49397] [AC:U49397][PN:unknown] [OR:Streptococcus pyogenes] 79 SPX1670 1670 4331 63 189NO-HIT 6 SPX1671 1671 4332 222 666 235 4.10E-25 [GI:558538] [LN:SUHSAPI][AC:D38490] [PN:sperm-activating peptide I precursor] [OR:Hemicentrotuspulcherrimus] [SR:Hemicentrotus pulcherrimus female ovary accessory cell(library] 179 SPX1672 1672 4333 451 1353 500 6.50E-65 [GI:4838563][LN:AF145055] [AC:AF145055] [PN:surface protein C PspC][OR:Streptococcus pneumoniae] 98 SPX1673 1673 4334 183 549 213 1.70E-21[GI:7293488] [LN:AE003509] [AC:AE003509:AE002593] [GN:CG15040][OR:Drosophila melanogaster] [SR:fruit fly] 106 SPX1674 1674 4335 176528 112 1.00E-08 [GI:406446] [LN:MGU02192] [AC:U02192] [OR:Mycoplasmagenitalium] 64 SPX1675 1675 4336 182 546 107 1.20E-15 [GI:3849798][LN:U91581] [AC:U91581:U04057] [PN:putative transposase] [GN:tpase][OR:Lactococcus lactis subsp. lactis] 118 SPX1676 1676 4337 251 753 1757.10E-43 [GI:6746427] [LN:AF179847] [AC:AF179847] [PN:putativetransposase] [OR:Lactococcus lactis] 90 SPX1677 1677 4338 65 195 NO-HIT6 SPX1678 1678 4339 55 165 183 1.50E-19 [GI:2576331] [LN:SPSPSA2][AC:AJ002054] [PN:SpsA protein] [FN:IgA binding protein][OR:Streptococcus pneumoniae] 112 SPX1679 1679 4340 419 1257 20391.30E-284 [GI:2804700] [LN:AF030361] [AC:AF030361] [PN:transposase][OR:Streptococcus pneumoniae] 87 SPX1680 1680 4341 232 696 12961.20E-171 [GI:4097980] [LN:SPU72655] [AC:U72655] [PN:surface protein C][GN:pspC] [OR:Streptococcus pneumoniae] 101 SPX1681 1681 4342 110 330NO-HIT 6 SPX1682 1682 4343 105 315 98 7.50E-05 [LN:T14867] [AC:T14867][PN:interaptin] [GN:abpD] [OR:Dictyostelium discoideum] 79 SPX1683 16834344 217 651 599 1.00E-117 [GI:6469845] [LN:AF068645] [AC:AF068645][PN:unknown] [GN:pspC] [OR:Streptococcus pneumoniae] 93 SPX1684 16844345 73 219 66 0.001 [GI:340613] [LN:LEIKPMURF2] [AC:L07545] [GN:MURF2][OR:Kinetoplast Leishmania tarentolae] [SR:Kinetoplast Leishmaniatarentolae (strain UC, organelle Kinetoplas] 163 SPX1685 1685 4346 105315 94 1.40E-05 [LN:YHU3_YEAST] [AC:P38844] [GN:YHR143W][OR:Saccharomyces cerevisiae] [SR:,Baker′s yeast] [DE:PRECURSOR][SP:P38844] 119 SPX1686 1686 4347 276 828 697 7.60E-123 [GI:2576333][LN:SPSPSA47] [AC:AJ002055] [PN:SpsA protein] [FN:IgA binding protein][OR:Streptococcus pneumoniae] 113 SPX1687 1687 4348 176 528 382 1.80E-50[LN:F81147] [AC:F81147] [PN:conserved hypothetical protein NMB0883[imported]] [GN:NMB0883] [OR:Neisseria meningitidis] 119 SPX1688 16884349 447 1341 1245 0 [GI:5830533] [LN:SPAJ6395] [AC:AJ006395][PN:histidine kinase] [GN:hk06] [OR:Streptococcus pneumoniae] 102SPX1689 1689 4350 218 654 1100 3.60E-150 [GI:5830532] [LN:SPAJ6395][AC:AJ006395] [PN:response regulator] [GN:rr06] [OR:Streptococcuspneumoniae] 104 SPX1690 1690 4351 75 225 NO-HIT 6 SPX1691 1691 4352 8112433 1102 3.30E-266 [GI:4103472] [LN:AF023422] [AC:AF023422] [PN:ClpC][GN:clpC] [OR:Lactococcus lactis] 84 SPX1692 1692 4353 174 522 3234.90E-44 [LN:LLA249133] [AC:AJ249133] [PN:CtsR protein] [GN:ctsR][FN:transcriptional regulator] [OR:Lactococcus lactis] 111 SPX1693 16934354 243 729 255 1.80E-47 [LN:B72369] [AC:B72369] [PN:ABC transporter,ATP-binding protein] [GN:TM0483] [CL:unassigned ATP-binding cassetteproteins:ATP-binding cassette homology] [OR:Thermotoga maritima] 180SPX1694 1694 4355 336 1008 561 9.10E-87 [LN:C72369] [AC:C72369][PN:hypothetical protein TM0484] [GN:TM0484] [OR:Thermotoga maritima] 93SPX1695 1695 4356 136 408 NO-HIT 6 SPX1696 1696 4357 250 750 4401.10E-58 [LN:D72369] [AC:D72369] [PN:ABC transporter, permease protein,cysTW family] [GN:TM0485] [CL:Synechococcus nitrate transport proteinnrtB] [OR:Thermotoga maritima] 165 SPX1697 1697 4358 97 291 118 4.00E-14[LN:YVI2_CLOPE] [AC:Q46213] [OR:Clostridium perfringens][DE:HYPOTHETICAL 10.7 KD PROTEIN IN VIRR 5′REGION (ORF2)] [SP:Q46213]126 SPX1698 1698 4359 284 852 319 8.30E-35 [LN:S57721] [AC:S57721][PN:cspB protein] [CL:cpl repeat homology] [OR:Clostridiumacetobutylicum] 98 SPX1699 1699 4360 138 414 102 7.10E-06 [GI:1340128][LN:SA1234] [AC:X97985] [OR:Staphylococcus aureus] 63 SPX1700 1700 436189 267 72 3.10E-05 [LN:VEG_BACSU] [AC:P37466] [GN:VEG] [OR:Bacillussubtilis] [DE:VEG PROTEIN] [SP:P37466] 87 SPX1701 1701 4362 451 1353 8271.60E-171 [LN:DNAC_BACSU] [AC:P37469] [GN:DNAC] [OR:Bacillus subtilis][EC:3.6.1.-] [DE:REPLICATIVE DNA HELICASE,] [SP:P37469] 118 SPX1702 17024363 151 453 193 1.20E-44 [LN:RL9_BACST] [AC:P02417] [GN:RPLI][OR:Bacillus stearothermophilus] [DE:50S RIBOSOMAL PROTEIN L9 (BL17)][SP:P02417] 118 SPX1703 1703 4364 658 1974 301 6.60E-68 [LN:YYBT_BACSU][AC:P37484] [GN:YYBT] [OR:Bacillus subtilis] [DE:HYPOTHETICAL 74.3 KDPROTEIN IN RPLI-COTF INTERGENIC REGION] [SP:P37484] 137 SPX1704 17044365 183 549 358 5.10E-68 [LN:LLA249134] [AC:AJ249134] [PN:hypotheticalprotein] [OR:Lactococcus lactis] 78 SPX1705 1705 4366 221 663 1432.90E-23 [LN:CMF3_BACSU] [AC:P39147] [GN:COMFC:COMF3] [OR:Bacillussubtilis] [DE:COMF OPERON PROTEIN 3] [SP:P39147] 106 SPX1706 1706 4367433 1299 269 2.00E-31 [LN:CMF1_BACSU] [AC:P39145] [GN:COMFA:COMF1][OR:Bacillus subtilis] [DE:COMF OPERON PROTEIN 1] [SP:P39145] 106SPX1707 1707 4368 212 636 475 1.00E-60 [LN:YVYE_BACSU][AC:P32437:P96500] [GN:YVYE:YVHK] [OR:Bacillus subtilis][DE:HYPOTHETICAL 24.8 KD PROTEIN IN DEGS-TAGO INTERGENIC REGION][SP:P32437:P96500] 156 SPX1708 1708 4369 309 927 1289 7.30E-171[GI:6567187] [LN:AB028865] [AC:AB028865] [PN:O-acetylserine lyase][GN:cysM] [OR:Streptococcus suis] [SR:Streptococcus suis (strain:SMR)DNA] 141 SPX1709 1709 4370 347 1041 498 1.10E-82 [LN:EFTS_BACSU][AC:P80700:O31748] [GN:TSF] [OR:Bacillus subtilis] [DE:ELONGATION FACTORTS (EF-TS)] [SP:P80700:O31748] 119 SPX1710 1710 4371 129 387 NO-HIT 6SPX1711 1711 4372 288 864 1013 1.60E-15 [LN:RS2_PEDAC] [AC:P49668][GN:RPSB] [OR:Pediococcus acidilactici] [DE:30S RIBOSOMAL PROTEIN S2][SP:P49668] 108 SPX1712 1712 4373 75 225 NO-HIT 6 SPX1713 1713 4374 3931179 459 3.30E-76 [LN:JN0097] [AC:JN0097] [PN:secreted 45K proteinprecursor] [OR:Lactococcus lactis] 83 SPX1714 1714 4375 80 240 NO-HIT 6SPX1715 1715 4376 165 495 108 7.90E-08 [LN:MRED_BACSU] [AC:Q01467][GN:MRED:RODB] [OR:Bacillus subtilis] [DE:ROD SHAPE-DETERMINING PROTEINMRED] [SP:Q01467] 117 SPX1716 1716 4377 273 819 141 1.60E-17[LN:MREC_BACSU] [AC:Q01466] [GN:MREC] [OR:Bacillus subtilis] [DE:RODSHAPE-DETERMINING PROTEIN MREC] [SP:Q01466] 112 SPX1717 1717 4378 265795 694 1.30E-95 [LN:F69742] [AC:F69742] [PN:hypothetical protein ybaF][GN:ybaF] [OR:Bacillus subtilis] 87 SPX1718 1718 4379 57 171 NO-HIT 6SPX1719 1719 4380 280 840 623 4.20E-94 [LN:E69742] [AC:E69742] [PN:ABCtransporter (ATP-binding protein) homolog ybaE] [GN:ybaE] [CL:unassignedATP-binding cassette proteins:ATP-binding cassette homology][OR:Bacillus subtilis] 188 SPX1720 1720 4381 116 348 127 7.40E-11[LN:C71234] [AC:C71234] [PN:hypothetical protein PH0133] [GN:PH0133][OR:Pyrococcus horikoshii] 95 SPX1721 1721 4382 262 786 853 1.50E-116[GI:3426368] [LN:AF082738] [AC:AF082738] [PN:ABC transporter ATP-bindingprotein] [GN:stpA] [OR:Streptococcus pyogenes] 119 SPX1722 1722 4383 75225 106 1.30E-09 [LN:A71007] [AC:A71007] [PN:hypothetical proteinPH1351] [GN:PH1351] [OR:Pyrococcus horikoshii] 95 SPX1723 1723 4384 182546 531 6.40E-72 [GI:3426367] [LN:AF082738] [AC:AF082738][PN:phosphotidylglycerophosphate synthase] [GN:pgsA] [OR:Streptococcuspyogenes] 121 SPX1724 1724 4385 277 831 100 1.50E-21 [GI:3426366][LN:AF082738] [AC:AF082738] [PN:unknown] [OR:Streptococcus pyogenes] 81SPX1725 1725 4386 428 1284 403 1.10E-102 [GI:3426365] [LN:AF082738][AC:AF082738] [PN:unknown] [OR:Streptococcus pyogenes] 81 SPX1726 17264387 417 1251 694 2.70E-103 [GI:3426364] [LN:AF082738] [AC:AF082738][PN:unknown] [OR:Streptococcus pyogenes] 81 SPX1727 1727 4388 123 369148 1.20E-26 [LN:JC4754] [AC:JC4754] [PN:hypothetical 13.6k protein][GN:recF] [OR:Lactococcus lactis] 89 SPX1728 1728 4389 366 1098 11271.20E-163 [LN:RECF_STRPY] [AC:P49999] [GN:RECF] [OR:Streptococcuspyogenes] [DE:RECF PROTEIN] [SP:P49999] 95 SPX1729 1729 4390 493 14792283 0 [LN:IMDH_STRPY] [AC:P50099] [GN:GUAB] [OR:Streptococcus pyogenes][EC:1.1.1.205] [DE:DEHYDROGENASE) (IMPDH) (IMPD)] [SP:P50099] 127SPX1730 1730 4391 49 147 99 1.30E-07 [LN:F71456] [AC:F71456][PN:hypothetical protein PH0308] [GN:PH0308] [OR:Pyrococcus horikoshii]95 SPX1731 1731 4392 342 1026 672 2.00E-153 [LN:SYW_CLOLO] [AC:Q46127][GN:TRPS:TRSA] [OR:Clostridium longisporum] [EC:6.1.1.2] [DE:(TRPRS)][SP:Q46127] 108 SPX1732 1732 4393 541 1623 1364 9.40E-252 [LN:E69861][AC:E69861] [PN:ABC transporter (ATP-binding protein) homolog ykpA][GN:ykpA] [CL:unassigned ATP-binding cassette proteins:ATP-bindingcassette homology] [OR:Bacillus subtilis] 188 SPX1733 1733 4394 851 2553503 1.40E-88 [GI:3043878] [LN:LLU95840] [AC:U95840] [PN:transmembraneprotein Tmp5] [OR:Lactococcus lactis] 94 SPX1734 1734 4395 105 315 1815.50E-19 [LN:YHGE_BACSU] [AC:P32399] [GN:YHGE] [OR:Bacillus subtilis][DE:HYPOTHETICAL 84.1 KD PROTEIN IN HEMY-GLTT INTERGENIC REGION (ORFB)][SP:P32399] 144 SPX1735 1735 4396 113 339 138 1.10E-11 [LN:YHGE_BACSU][AC:P32399] [GN:YHGE] [OR:Bacillus subtilis] [DE:HYPOTHETICAL 84.1 KDPROTEIN IN HEMY-GLTT INTERGENIC REGION (ORFB)] [SP:P32399] 144 SPX17361736 4397 256 768 307 2.50E-46 [GI:3043882] [LN:LLU95842] [AC:U95842][PN:transmembrane protein Tmp7] [OR:Lactococcus lactis] 94 SPX1737 17374398 181 543 98 5.30E-09 [GI:6899263] [LN:AE002125][AC:AE002125:AF222894] [PN:unique hypothetical] [GN:UU290][OR:Ureaplasma urealyticum] 113 SPX1738 1738 4399 251 753 1294 2.50E-176[GI:1613769] [LN:SPU33315] [AC:U33315] [PN:response regulator] [GN:comE][OR:Streptococcus pneumoniae] 102 SPX1739 1739 4400 442 1326 2246 0[GI:1613768] [LN:SPU33315] [AC:U33315] [PN:histidine protein kinase][GN:comD] [OR:Streptococcus pneumoniae] 108 SPX1740 1740 4401 160 480781 4.50E-104 [GI:2109449] [LN:SPDNAARG] [AC:AF000658] [FN:unknown][OR:Streptococcus pneumoniae] 83 SPX1741 1741 4402 398 1194 19638.90E-259 [GI:2109443] [LN:SPDNAARG] [AC:AF000658] [PN:putative serineprotease] [GN:sphtra] [OR:Streptococcus pneumoniae] 112 SPX1742 17424403 253 759 1225 5.80E-163 [GI:2109444] [LN:SPDNAARG] [AC:AF000658][PN:SPSpoJ] [GN:spspoJ] [FN:unknown] [OR:Streptococcus pneumoniae] 107SPX1743 1743 4404 454 1362 2287 0 [LN:DNAA_STRPN] [AC:O08397] [GN:DNAA][OR:Streptococcus pneumoniae] [DE:CHROMOSOMAL REPLICATION INITIATORPROTEIN DNAA] [SP:O08397] 131 SPX1744 1744 4405 379 1137 1857 2.90E-250[LN:DP3B_STRPN] [AC:O06672] [GN:DNAN] [OR:Streptococcus pneumoniae][EC:2.7.7.7] [DE:DNA POLYMERASE III, BETA CHAIN,] [SP:O06672] 131SPX1745 1745 4406 65 195 339 1.60E-43 [GI:2109447] [LN:SPDNAARG][AC:AF000658] [FN:unknown] [OR:Streptococcus pneumoniae] 83 SPX1746 17464407 375 1125 710 9.10E-176 [LN:YYAF_BACSU] [AC:P37518] [GN:YYAF][OR:Bacillus subtilis] [DE:REGION] [SP:P37518] 84 SPX1747 1747 4408 190570 368 3.70E-62 [LN:SP5C_BACSU] [AC:P37470] [GN:SPOVC:PTH] [OR:Bacillussubtilis] [EC:3.1.1.29] [DE:SPORULATION PROTEIN C)] [SP:P37470] 119SPX1748 1748 4409 1170 3510 2088 0 [GI:3511015] [LN:AF054624][AC:AF054624] [PN:transcription-repair coupling factor] [GN:mfd][OR:Lactobacillus sakei] 116 SPX1749 1749 4410 99 297 NO-HIT 6 SPX17501750 4411 89 267 275 3.50E-33 [LN:YABO_BACSU] [AC:P37557] [GN:YABO][OR:Bacillus subtilis] [DE:HYPOTHETICAL 9.7 KD PROTEIN IN MFD-DIVICINTERGENIC REGION] [SP:P37557] 136 SPX1751 1751 4412 123 369 1121.50E-08 [GI:4090866] [LN:AF023181] [AC:AF023181] [PN:DivIC homolog][GN:divL] [OR:Listeria monocytogenes] 97 SPX1752 1752 4413 74 222 NO-HIT6 SPX1753 1753 4414 446 1338 NO-HIT 6 SPX1754 1754 4415 426 1278 1286.70E-28 [LN:D72358] [AC:D72358] [PN:conserved hypothetical protein][GN:TM0579] [CL:hypothetical protein HI0404] [OR:Thermotoga maritima]129 SPX1755 1755 4416 181 543 374 1.10E-80 [LN:HPRT_LACLA] [AC:Q02522][GN:HPT] [OR:Lactococcus lactis] [SR:,subsplactis:Streptococcus lactis][EC:2.4.2.8] [DE:(HGPRTASE)] [SP:Q02522] 142 SPX1756 1756 4417 653 19593277 0 [GI:5030426] [LN:AF061748] [AC:AF061748] [PN:cell divisionprotein FtsH] [GN:ftsH] [OR:Streptococcus pneumoniae] 112 SPX1757 17574418 208 624 181 9.80E-25 [LN:A71115] [AC:A71115] [PN:hypotheticalprotein PH0688] [GN:PH0688] [OR:Pyrococcus horikoshii] 95 SPX1758 17584419 36 108 NO-HIT 6 SPX1759 1759 4420 160 480 844 9.40E-114[GI:5739312] [LN:AF161700] [AC:AF161700] [PN:ComX1] [GN:comX1][FN:transcriptional regulator of] [OR:Streptococcus pneumoniae] 126SPX1760 1760 4421 82 246 NO-HIT 6 SPX1761 1761 4422 50 150 82 7.60E-06[LN:G71244] [AC:G71244] [PN:hypothetical protein PH0217] [GN:PH0217][OR:Pyrococcus horikoshii] 95 SPX1762 1762 4423 62 186 NO-HIT 6 SPX17631763 4424 87 261 136 3.90E-14 [LN:G81516] [AC:G81516] [PN:hypotheticalprotein CP0988 [imported]] [GN:CP0988] [OR:Chlamydophilapneumoniae:Chlamydia pneumoniae] 130 SPX1764 1764 4425 136 408 NO-HIT 6SPX1765 1765 4426 52 156 NO-HIT 6 SPX1766 1766 4427 52 156 87 3.30E-06[LN:D75542] [AC:D75542] [PN:hypothetical protein] [GN:DR0254][OR:Deinococcus radiodurans] 90 SPX1767 1767 4428 82 246 247 1.10E-29[LN:F81737] [AC:F81737] [PN:hypothetical protein TC0129 [imported]][GN:TC0129] [OR:Chlamydia muridarum:Chlamydia trachomatis MoPn] 131SPX1768 1768 4429 78 234 143 4.90E-15 [LN:F71245] [AC:F71245][PN:hypothetical protein PHS004] [GN:PHS004] [OR:Pyrococcus horikoshii]95 SPX1769 1769 4430 69 207 340 7.40E-44 [GI:5019553] [LN:SPN239004][AC:AJ239004] [PN:putative transposase] [OR:Streptococcus pneumoniae] 97SPX1770 1770 4431 82 246 256 1.40E-36 [GI:663279] [LN:STRCOMAA][AC:M36180:L15190] [PN:transposase] [OR:Streptococcus pneumoniae][SR:Streptococcus pneumoniae (strain RX1) DNA] 138 SPX1771 1771 4432 47141 119 1.30E-09 [GI:2804700] [LN:AF030361] [AC:AF030361][PN:transposase] [OR:Streptococcus pneumoniae] 87 SPX1772 1772 4433 91273 387 3.30E-50 [GI:663278] [LN:STRCOMAA] [AC:M36180:L15190][PN:transposase] [OR:Streptococcus pneumoniae] [SR:Streptococcuspneumoniae (strain RX1) DNA] 138 SPX1773 1773 4434 81 243 NO-HIT 6SPX1774 1774 4435 443 1329 1739 2.60E-235 [LN:A42280][AC:S65968:A42280:H69683] [PN:adenylosuccinate synthase,purA:IMP--aspartate ligase] [GN:purA] [CL:adenylosuccinate synthase][OR:Bacillus subtilis] [EC:6.3.4.4] 175 SPX1775 1775 4436 141 423 3651.90E-46 [LN:YAAJ_BACSU] [AC:P21335] [GN:YAAJ] [OR:Bacillus subtilis][DE:HYPOTHETICAL 17.8 KD PROTEIN IN SERS-DNAH INTERGENIC REGION][SP:P21335] 137 SPX1776 1776 4437 148 444 205 2.80E-38 [GI:2765131][LN:LLABIKORF] [AC:Y11901] [PN:dUTPase] [OR:Lactococcus lactis] 76SPX1777 1777 4438 186 558 NO-HIT 6 SPX1778 1778 4439 68 204 NO-HIT 6SPX1779 1779 4440 455 1365 1167 1.60E-201 [LN:RADA_BACSU] [AC:P37572][GN:RADA:SMS] [OR:Bacillus subtilis] [DE:DNA REPAIR PROTEIN RADA HOMOLOG(DNA REPAIR PROTEIN SMS HOMOLOG)] [SP:P37572] 146 SPX1780 1780 4441 207621 NO-HIT 6 SPX1781 1781 4442 166 498 268 2.80E-38 [LN:Y023_MYCTU][AC:Q10612] [GN:MTCY373.03] [OR:Mycobacterium tuberculosis][DE:HYPOTHETICAL 18.2 KD PROTEIN CY373.03] [SP:Q10612] 130 SPX1782 17824443 264 792 NO-HIT 6 SPX1783 1783 4444 323 969 607 9.40E-148[GI:532204] [LN:LISTMS] [AC:M92842] [GN:prs] [OR:Listeria monocytogenes][SR:Listeria monocytogenes (strain L028) DNA] 118 SPX1784 1784 4445 160480 493 3.90E-65 [GI:663278] [LN:STRCOMAA] [AC:M36180:L15190][PN:transposase] [OR:Streptococcus pneumoniae] [SR:Streptococcuspneumoniae (strain RX1) DNA] 138 SPX1785 1785 4446 113 339 NO-HIT 6SPX1786 1786 4447 122 366 NO-HIT 6 SPX1787 1787 4448 131 393 NO-HIT 6SPX1788 1788 4449 118 354 NO-HIT 6 SPX1789 1789 4450 890 2670 4412 0[LN:DPO1_STRPN] [AC:P13252] [GN:POLA] [OR:Streptococcus pneumoniae][EC:2.7.7.7] [DE:DNA POLYMERASE I, (POL I)] [SP:P13252] 125 SPX1790 17904451 124 372 181 3.30E-32 [LN:B69892] [AC:B69892] [PN:conservedhypothetical protein yneT] [GN:yneT] [CL:hypothetical protein yneT][OR:Bacillus subtilis] 128 SPX1791 1791 4452 137 411 328 2.80E-41[LN:T30285] [AC:T30285] [PN:hypothetical protein] [OR:Streptococcuspneumoniae] 79 SPX1792 1792 4453 105 315 83 0.00036 [LN:T30285][AC:T30285] [PN:hypothetical protein] [OR:Streptococcus pneumoniae] 79SPX1793 1793 4454 239 717 398 3.00E-50 [LN:YOR3_BACCE] [AC:O31352][OR:Bacillus cereus] [DE:HYPOTHETICAL PROTEIN (ORF3) (FRAGMENT)][SP:O31352] 104 SPX1794 1794 4455 171 513 212 5.40E-30 [LN:YF05_METTH][AC:O27549] [GN:MTH1505] [OR:Methanobacterium thermoautotrophicum][DE:HYPOTHETICAL PROTEIN MTH1505] [SP:O27549] 128 SPX1795 1795 4456 126378 NO-HIT 6 SPX1796 1796 4457 167 501 456 2.50E-57 [LN:RL10_BACSU][AC:P42923] [GN:RPLJ] [OR:Bacillus subtilis] [DE:(VEGETATIVE PROTEIN300) (VEG300)] [SP:P42923] 111 SPX1797 1797 4458 123 369 255 1.30E-46[LN:RL7_MICLU] [AC:P02395] [GN:RPLL] [OR:Micrococcus luteus][SR:,Micrococcus lysodeikticus] [DE:50S RIBOSOMAL PROTEIN L7/L12(MA1/MA2)] [SP:P02395] 150 SPX1798 1798 4459 115 345 98 1.30E-05[LN:T40374] [AC:T40374] [PN:hypothetical protein SPBC3D6.14c][OR:Schizosaccharomyces pombe] 92 SPX1799 1799 4460 196 588 NO-HIT 6SPX1800 1800 4461 505 1515 214 1.60E-47 [LN:T35180] [AC:T35180][PN:hypothetical protein SC5A7.31] [GN:SC5A7.31] [CL:Streptomycescoelicolor hypothetical protein SC5A7.31] [OR:Streptomyces coelicolor]160 SPX1801 1801 4462 198 594 136 6.60E-20 [GI:290801] [LN:FRNVALAB][AC:L17003] [GN:valA] [OR:Francisella tularensis var. novicida][SR:Francisella novicida (strain U112) DNA] 133 SPX1802 1802 4463 97 291NO-HIT 6 SPX1803 1803 4464 247 741 357 1.50E-55 [GI:7288062] [LN:SCD40A][AC:AL161691] [PN:putative ABC-transporter ATP-binding protein][GN:SCD40A.12c] [OR:Streptomyces coelicolor A3(2)] 139 SPX1804 1804 446560 180 NO-HIT 6 SPX1805 1805 4466 129 387 90 6.90E-06 [LN:F72598][AC:F72598] [PN:hypothetical protein APE1254] [GN:APE1254] [OR:Aeropyrumpernix] 92 SPX1806 1806 4467 440 1320 NO-HIT 6 SPX1807 1807 4468 60 180NO-HIT 6 SPX1808 1808 4469 74 222 NO-HIT 6 SPX1809 1809 4470 45 135 1093.10E-09 [LN:Y4PE_RHISN] [AC:P55614] [GN:Y4PE,Y4SA] [OR:Rhizobium sp][SR:,strain NGR234] [DE:HYPOTHETICAL 15.5 KD PROTEIN Y4PE/Y4SA][SP:P55614] 138 SPX1810 1810 4471 88 264 301 4.50E-37 [LN:S52544][AC:S52544] [PN:ISL2 protein] [OR:Lactobacillus helveticus] 71 SPX18111811 4472 233 699 331 2.60E-64 [LN:C70180] [AC:C70180] [PN:conservedhypothetical protein BB0644] [OR:Borrelia burgdorferi] [SR:, Lymedisease spirochete] 125 SPX1812 1812 4473 308 924 98 4.30E-21[LN:I40867] [AC:I40867] [PN:hypothetical protein 2] [OR:Clostridiumperfringens] 80 SPX1813 1813 4474 543 1629 102 3.10E-21 [LN:B71130][AC:B71130] [PN:probable oligopeptide binding protein APPA] [GN:PH0807][CL:dipeptide transport protein] [OR:Pyrococcus horikoshii] 143 SPX18141814 4475 317 951 335 2.30E-78 [LN:D75202] [AC:D75202] [PN:dipeptide abctransporter, dipeptide-binding protein PAB0092] [GN:dppB-1:PAB0092][CL:transmembrane protein dppB] [OR:Pyrococcus abyssi] 166 SPX1815 18154476 296 888 642 5.70E-87 [LN:APPC_BACSU] [AC:P42063] [GN:APPC][OR:Bacillus subtilis] [DE:OLIGOPEPTIDE TRANSPORT PERMEASE PROTEIN APPC][SP:P42063] 122 SPX1816 1816 4477 204 612 NO-HIT 6 SPX1817 1817 4478 6611983 644 1.60E-146 [LN:YLIA_ECOLI] [AC:P75796] [GN:YLIA] [OR:Escherichiacoli] [DE:HYPOTHETICAL ABC TRANSPORTER ATP-BINDING PROTEIN YLIA][SP:P75796] 130 SPX1818 1818 4479 66 198 NO-HIT 6 SPX1819 1819 4480 4701410 NO-HIT 6 SPX1820 1820 4481 163 489 450 8.60E-58 [LN:YUTG_BACSU][AC:O32124] [GN:YUTG] [OR:Bacillus subtilis] [DE:HYPOTHETICAL 18.7 KDPROTEIN IN HOM-MRGA INTERGENIC REGION] [SP:O32124] 136 SPX1821 1821 4482136 408 190 1.30E-38 [LN:CDD_BACSU] [AC:P19079] [GN:CDD] [OR:Bacillussubtilis] [EC:3.5.4.5] [DE:CYTIDINE DEAMINASE, (CYTIDINE AMINOHYDROLASE)(CDA)] [SP:P19079] 142 SPX1822 1822 4483 95 285 NO-HIT 6 SPX1823 18234484 274 822 771 1.10E-101 [GI:2385360] [LN:CTSIALIDA] [AC:Y08695][PN:putative acylneuraminate lyase] [OR:Clostridium tertium] 100 SPX18241824 4485 68 204 173 1.10E-18 [LN:S43901] [AC:S43901:S27537][PN:hypothetical protein A] [OR:Clostridium perfringens] 87 SPX1825 18254486 173 519 145 3.80E-20 [GI:2668605] [LN:AF015453] [AC:AF015453][PN:unknown] [OR:Lactobacillus rhamnosus] 82 SPX1826 1826 4487 214 642509 7.20E-64 [GI:6318176] [LN:BSP250862] [AC:AJ250862] [PN:MrsT protein][GN:mrsT] [FN:putative ABC-transporter] [OR:Bacillus sp. HIL-Y85/54728]131 SPX1827 1827 4488 63 189 NO-HIT 6 SPX1828 1828 4489 449 1347 7315.00E-191 [GI:3702805] [LN:AF056335] [AC:AF056335] [PN:NADP-specificglutamate dehydrogenase] [GN:gdhA] [OR:Bacillus licheniformis] 121SPX1829 1829 4490 138 414 99 6.40E-06 [LN:S31840] [AC:S31840][PN:probable transposase] [OR:Bacillus stearothermophilus] 82 SPX18301830 4491 57 171 94 3.30E-07 [LN:Y4PE_RHISN] [AC:P55614] [GN:Y4PE,Y4SA][OR:Rhizobium sp] [SR:,strain NGR234] [DE:HYPOTHETICAL 15.5 KD PROTEINY4PE/Y4SA] [SP:P55614] 138 SPX1831 1831 4492 218 654 154 1.00E-20[GI:722339] [LN:AXU22323] [AC:U22323] [PN:unknown] [OR:Acetobacterxylinus] [SR:Acetobacter xylinum] 100 SPX1832 1832 4493 73 219 NO-HIT 6SPX1833 1833 4494 95 285 146 8.10E-34 [GI:4193373] [LN:AF072894][AC:AF072894] [PN:ribosomal protein L31] [GN:rpmE] [OR:Listeriamonocytogenes] 105 SPX1834 1834 4495 312 936 397 7.80E-97 [LN:F69999][AC:F69999] [PN:conserved hypothetical protein ytqI] [GN:ytqI][CL:Mycoplasma conserved hypothetical protein MG190] [OR:Bacillussubtilis] 150 SPX1835 1835 4496 145 435 271 2.00E-32 [LN:FLAV_BACSU][AC:O34737] [GN:YKUN] [OR:Bacillus subtilis] [DE:PROBABLE FLAVODOXIN 1][SP:O34737] 99 SPX1836 1836 4497 89 267 117 2.80E-11 [LN:Y246_METJA][AC:Q57696] [GN:MJ0246] [OR:Methanococcus jannaschii] [DE:HYPOTHETICALPROTEIN MJ0246] [SP:Q57696] 114 SPX1837 1837 4498 125 375 169 5.60E-18[LN:C75108] [AC:C75108] [PN:crcb protein PAB1925] [GN:PAB1925][CL:hypothetical protein MJ1523] [OR:Pyrococcus abyssi] 118 SPX1838 18384499 110 330 93 1.20E-10 [LN:B71026] [AC:B71026] [PN:hypotheticalprotein PH1502] [GN:PH1502] [CL:hypothetical protein MJ1523][OR:Pyrococcus horikoshii] 128 SPX1839 1839 4500 116 348 537 4.70E-71[LN:RL19_STRTR] [AC:O34031] [GN:RPLS] [OR:Streptococcus thermophilus][DE:50S RIBOSOMAL PROTEIN L19] [SP:O34031] 112 SPX1840 1840 4501 269 807354 2.70E-85 [LN:YIDA_ECOLI] [AC:P09997:P76737] [GN:YIDA][OR:Escherichia coli] [DE:HYPOTHETICAL 29.7 KD PROTEIN IN IBPA-GYRBINTERGENIC REGION] [SP:P09997:P76737] 150 SPX1841 1841 4502 448 1344 5612.90E-126 [LN:YWFO_BACSU] [AC:P39651] [GN:YWFO:IPA-93D] [OR:Bacillussubtilis] [DE:HYPOTHETICAL 51.0 KD PROTEIN IN PTA 3′REGION] [SP:P39651]130 SPX1842 1842 4503 126 378 NO-HIT 6 SPX1843 1843 4504 111 333 4993.70E-65 [GI:1850606] [LN:SMU88582] [AC:U88582] [PN:YlxM] [GN:ylxM][FN:unknown] [OR:Streptococcus mutans] 97 SPX1844 1844 4505 185 555NO-HIT 6 SPX1845 1845 4506 524 1572 1993 5.90E-290 [LN:SR54_STRMU][AC:Q54431:P96469] [GN:FFH] [OR:Streptococcus mutans] [DE:SIGNALRECOGNITION PARTICLE PROTEIN (FIFTY-FOUR HOMOLOG)] [SP:Q54431:P96469]150 SPX1846 1846 4507 163 489 NO-HIT 6 SPX1847 1847 4508 257 771 5001.10E-87 [LN:PYRP_BACCL] [AC:P41006] [GN:PYRP] [OR:Bacilluscaldolyticus] [DE:URACIL PERMEASE (URACIL TRANSPORTER)] [SP:P41006] 118SPX1848 1848 4509 147 441 231 5.00E-42 [LN:LLA132624] [AC:AJ132624][PN:uracil transporter] [GN:pyrP] [OR:Lactococcus lactis] 86 SPX18491849 4510 238 714 353 3.70E-81 [LN:GIDB_BACSU] [AC:P25813] [GN:GIDB][OR:Bacillus subtilis] [DE:GLUCOSE INHIBITED DIVISION PROTEIN B][SP:P25813] 114 SPX1850 1850 4511 187 561 261 1.60E-57 [GI:1519287][LN:LMU66186] [AC:U66186] [PN:LemA] [GN:lemA] [OR:Listeriamonocytogenes] 86 SPX1851 1851 4512 303 909 757 1.70E-165[LN:HTPX_STRGC] [AC:O30795] [GN:HTPX] [OR:Streptococcus gordoniichallis] [DE:PUTATIVE HEAT SHOCK PROTEIN HTPX] [SP:O30795] 123 SPX18521852 4513 520 1560 197 1.40E-47 [LN:YHES_ECOLI] [AC:P45535] [GN:YHES][OR:Escherichia coli] [DE:HYPOTHETICAL ABC TRANSPORTER ATP-BINDINGPROTEIN YHES] [SP:P45535] 130 SPX1853 1853 4514 92 276 NO-HIT 6 SPX18541854 4515 122 366 NO-HIT 6 SPX1855 1855 4516 181 543 64 6.40E-07[LN:C69875] [AC:C69875] [PN:hypothetical protein ylbN] [GN:ylbN][OR:Bacillus subtilis] 87 SPX1856 1856 4517 62 186 NO-HIT 6 SPX1857 18574518 210 630 446 2.10E-57 [LN:END3_BACSU] [AC:P39788] [GN:NTH:JOOB][OR:Bacillus subtilis] [EC:4.2.99.18] [DE:APYRIMIDINIC SITE) LYASE)][SP:P39788] 122 SPX1858 1858 4519 174 522 626 4.30E-82 [LN:LLA132624][AC:AJ132624] [PN:pyrimidine regulatory protein] [GN:pyrR] [FN:Regulatesexpression of the pyrimidine] [OR:Lactococcus lactis] 141 SPX1859 18594520 308 924 942 6.40E-134 [LN:LLA132624] [AC:AJ132624] [PN:aspartatetranscarbamoylase] [GN:pyrB] [OR:Lactococcus lactis] 95 SPX1860 18604521 360 1080 1492 2.60E-202 [LN:LLA132624] [AC:AJ132624] [PN:carbamoylphosphate synthetase small subunit] [GN:carA] [OR:Lactococcus lactis]112 SPX1861 1861 4522 1059 3177 4000 0 [GI:2598551] [LN:LLAJ109][AC:AJ000109] [PN:carbamoylphosphate synthetase] [GN:carB][OR:Lactococcus lactis] 108 SPX1862 1862 4523 70 210 NO-HIT 6 SPX18631863 4524 281 843 1425 1.90E-195 [GI:5001693] [LN:AF106539][AC:AF106539] [PN:LicD2] [GN:licD2] [OR:Streptococcus pneumoniae] 92SPX1864 1864 4525 268 804 1419 6.40E-194 [GI:5001692] [LN:AF106539][AC:AF106539] [PN:LicD1] [GN:licD1] [OR:Streptococcus pneumoniae] 92SPX1865 1865 4526 496 1488 2483 0 [GI:5001691] [LN:AF106539][AC:AF106539] [PN:unknown] [OR:Streptococcus pneumoniae] 83 SPX1866 18664527 236 708 96 7.30E-17 [LN:S60902] [AC:S60902:S49238:S44071][PN:CDP-ribitol pyrophosphorylase] [OR:Haemophilus influenzae] 100SPX1867 1867 4528 347 1041 66 6.20E-05 [LN:YJJN_ECOLI] [AC:P39400][GN:YJJN] [OR:Escherichia coli] [DE:INTERGENIC REGION] [SP:P39400] 94SPX1868 1868 4529 290 870 1361 2.10E-181 [GI:2708632] [LN:AF036951][AC:AF036951] [PN:choline kinase] [GN:pck] [OR:Streptococcus pneumoniae]99 SPX1869 1869 4530 293 879 156 1.70E-15 [LN:LICB_HAEIN][AC:P14182:Q57357:O05075] [GN:LICB:HI1538] [OR:Haemophilus influenzae][DE:LICB PROTEIN] [SP:P14182:Q57357:O05075] 130 SPX1870 1870 4531 230690 345 4.10E-54 [LN:D64128] [AC:D64128] [PN:lic-1 protein C] [GN:licC][OR:Haemophilus influenzae] 82 SPX1871 1871 4532 283 849 458 8.00E-59[LN:C72399] [AC:C72399] [PN:DNA processing chain A] [GN:TM0250][OR:Thermotoga maritima] 88 SPX1872 1872 4533 171 513 309 5.10E-41[LN:T30285] [AC:T30285] [PN:hypothetical protein] [OR:Streptococcuspneumoniae] 79 SPX1873 1873 4534 152 456 107 1.30E-07 [LN:T30285][AC:T30285] [PN:hypothetical protein] [OR:Streptococcus pneumoniae] 79SPX1874 1874 4535 69 207 NO-HIT 6 SPX1875 1875 4536 348 1044 1792.10E-23 [LN:Y678_METJA] [AC:Q58091] [GN:MJ0678] [OR:Methanococcusjannaschii] [DE:HYPOTHETICAL PROTEIN MJ0678] [SP:Q58091] 114 SPX18761876 4537 702 2106 1065 0 [LN:TOP1_BACSU] [AC:P39814] [GN:TOPA:TOPI][OR:Bacillus subtilis] [EC:5.99.1.2] [DE:(UNTWISTING ENZYME)(SWIVELASE)] [SP:P39814] 128 SPX1877 1877 4538 120 360 208 4.20E-25[LN:YBAN_ECOLI] [AC:P45808:P77478] [GN:YBAN] [OR:Escherichia coli][DE:HYPOTHETICAL 14.8 KD PROTEIN IN PRIC-APT INTERGENIC REGION][SP:P45808:P77478] 149 SPX1878 1878 4539 211 633 181 2.30E-34[GI:4680703] [LN:AF132966] [AC:AF132966] [PN:CGI-32 protein] [OR:Homosapiens] [SR:human] 89 SPX1879 1879 4540 219 657 142 3.40E-22[LN:YYAQ_BACSU] [AC:P37507] [GN:YYAQ] [OR:Bacillus subtilis][DE:HYPOTHETICAL 13.9 KD PROTEIN IN COTF-TETB INTERGENIC REGION][SP:P37507] 137 SPX1880 1880 4541 211 633 596 1.30E-93 [GI:2565151][LN:LLU92974] [AC:U92974:M90760:M90761] [PN:LeuA] [GN:leuA][OR:Lactococcus lactis] 96 SPX1881 1881 4542 70 210 NO-HIT 6 SPX18821882 4543 145 435 308 6.00E-39 [LN:LEU1_LACLA] [AC:Q02141] [GN:LEUA][OR:Lactococcus lactis] [SR:,subsplactis:Streptococcus lactis][EC:4.1.3.12] [DE:SYNTHASE) (ALPHA-IPM SYNTHETASE)] [SP:Q02141] 166SPX1883 1883 4544 346 1038 608 4.50E-153 [LN:LEU3_LACLA] [AC:Q02143][GN:LEUB] [OR:Lactococcus lactis] [SR:,subsplactis:Streptococcus lactis][EC:1.1.1.85] [DE:(IMDH) (3-IPM-DH)] [SP:Q02143] 151 SPX1884 1884 454590 270 129 8.30E-13 [LN:G69983] [AC:G69983] [PN:hypothetical proteinysdA] [GN:ysdA] [OR:Bacillus subtilis] 87 SPX1885 1885 4546 120 360 3739.40E-47 [LN:LEUD_LACLA] [AC:Q02144] [GN:LEUD] [OR:Lactococcus lactis][SR:,subsplactis:Streptococcus lactis] [EC:4.2.1.33][DE:(ISOPROPYLMALATE ISOMERASE) (ALPHA-IPM ISOMERASE)] [SP:Q02144] 183SPX1886 1886 4547 79 237 NO-HIT 6 SPX1887 1887 4548 89 267 NO-HIT 6SPX1888 1888 4549 645 1935 138 1.60E-33 [LN:MCRB_ECOLI] [AC:P15005][GN:MCRB:RGLB] [OR:Escherichia coli] [EC:3.1.21.-][DE:5-METHYLCYTOSINE-SPECIFIC RESTRICTION ENZYME B,] [SP:P15005] 145SPX1889 1889 4550 448 1344 96 4.40E-09 [LN:D81431] [AC:D81431][PN:hypothetical protein Cj0140 [imported]] [GN:Cj0140][OR:Campylobacter jejuni] 105 SPX1890 1890 4551 329 987 913 1.40E-171[LN:C70015] [AC:C70015] [PN:probable GMP reductase, yumD:guanosinemonophosphate reductase] [GN:yumD] [CL:GMP reductase:IMP dehydrogenaseamino-terminal homology:IMP dehydrogenase catalytic homology][OR:Bacillus subtilis] [EC:1.6.6.8] 237 SPX1891 1891 4552 78 234 NO-HIT6 SPX1892 1892 4553 67 201 NO-HIT 6 SPX1893 1893 4554 233 699 5381.70E-69 [LN:B69693] [AC:B69693:JC4821] [PN:ribonuclease III,:RNaseD:RNase O] [GN:rncS:srb] [CL:ribonuclease III:double-strandedRNA-binding repeat homology] [OR:Bacillus subtilis] [EC:3.1.26.3] 188SPX1894 1894 4555 737 2211 1258 7.10E-169 [LN:G69708][AC:G69708:JC4819:PC4029] [PN:chromosome segregation SMCprotein:minichromosome stabilizing protein SMC] [GN:smc] [CL:conservedhypothetical P115 protein] [OR:Bacillus subtilis] 189 SPX1895 1895 4556217 651 139 2.70E-09 [GI:2246532] [LN:U93872] [AC:U93872] [OR:Kaposi′ssarcoma-associated herpesvirus] [SR:Kaposi′s sarcoma-associatedherpesvirus - Human herpesvirus 8] 148 SPX1896 1896 4557 102 306 950.00014 [LN:P115_MYCHR] [AC:P41508] [OR:Mycoplasma hyorhinis] [DE:P115PROTEIN] [SP:P41508] 83 SPX1897 1897 4558 196 588 428 2.90E-69[LN:G69708] [AC:G69708:JC4819:PC4029] [PN:chromosome segregation SMCprotein:minichromosome stabilizing protein SMC] [GN:smc] [CL:conservedhypothetical P115 protein] [OR:Bacillus subtilis] 189 SPX1898 1898 4559265 795 206 4.40E-31 [GI:4062428] [LN:D90722] [AC:D90722:AB001340][PN:Hypothetical 30.2 kd protein in idh-deoR] [OR:Escherichia coli][SR:Escherichia coli(strain:K12) DNA, clone:Kohara clone #209] 178SPX1899 1899 4560 273 819 220 3.10E-42 [LN:YIDA_ECOLI][AC:P09997:P76737] [GN:YIDA] [OR:Escherichia coli] [DE:HYPOTHETICAL 29.7KD PROTEIN IN IBPA-GYRB INTERGENIC REGION] [SP:P09997:P76737] 150SPX1900 1900 4561 430 1290 675 1.30E-113 [GI:2633967] [LN:BSUB0009][AC:Z99112:AL009126] [PN:signal recognition particle (docking protein)][GN:ftsY] [FN:involved in secretion of extracellular proteins][OR:Bacillus subtilis] 184 SPX1901 1901 4562 419 1257 2039 1.30E-284[GI:2804700] [LN:AF030361] [AC:AF030361] [PN:transposase][OR:Streptococcus pneumoniae] 87 SPX1902 1902 4563 85 255 350 2.40E-45[GI:663279] [LN:STRCOMAA] [AC:M36180:L15190] [PN:transposase][OR:Streptococcus pneumoniae] [SR:Streptococcus pneumoniae (strain RX1)DNA] 138 SPX1903 1903 4564 109 327 288 1.40E-35 [GI:2804700][LN:AF030361] [AC:AF030361] [PN:transposase] [OR:Streptococcuspneumoniae] 87 SPX1904 1904 4565 173 519 858 5.70E-116 [GI:663278][LN:STRCOMAA] [AC:M36180:L15190] [PN:transposase] [OR:Streptococcuspneumoniae] [SR:Streptococcus pneumoniae (strain RX1) DNA] 138 SPX19051905 4566 496 1488 779 6.50E-166 [LN:G6PD_BACSU] [AC:P54547] [GN:ZWF][OR:Bacillus subtilis] [EC:1.1.1.49] [DE:PROTEIN 11) (VEG11)][SP:P54547] 110 SPX1906 1906 4567 247 741 772 4.80E-102 [LN:H69334][AC:H69334] [PN:glutamine transport protein glnQ] [GN:glnQ] [CL:innermembrane protein malK:ATP-binding cassette homology] [OR:Archaeoglobusfulgidus] 162 SPX1907 1907 4568 493 1479 508 2.50E-80 [GI:6560693][LN:AF141644] [AC:AF141644] [PN:putative integral membrane protein][FN:putative inner membrane component of a] [OR:Lactococcus lactis] 148SPX1908 1908 4569 237 711 91 0.00087 [LN:S76167] [AC:S76167][PN:hypothetical protein] [OR:Synechocystis sp.] [SR:PCC 6803, , PCC6803] [SR:PCC 6803, ] 116 SPX1909 1909 4570 90 270 80 4.20E-05[LN:T34651] [AC:T34651] [PN:probable transmembrane protein][GN:SC1A9.02] [OR:Streptomyces coelicolor] 102 SPX1910 1910 4571 6631989 3350 0 [LN:UVRB_STRPN] [AC:Q54986] [GN:UVRB:UVS402][OR:Streptococcus pneumoniae] [DE:EXCINUCLEASE ABC SUBUNIT B][SP:Q54986] 118 SPX1911 1911 4572 188 564 110 3.20E-15 [LN:G75474][AC:G75474] [PN:probable acetyltransferase] [GN:DR0796] [OR:Deinococcusradiodurans] 96 SPX1912 1912 4573 130 390 65 1.50E-06 [LN:T39482][AC:T39482] [PN:N-acetyltransferase] [GN:SPBC15D4.06] [CL:Escherichiacoli ribosomal-protein-alanine N-acetyltransferase rimI][OR:Schizosaccharomyces pombe] 169 SPX1913 1913 4574 156 468 1103.50E-09 [LN:G70031] [AC:G70031] [PN:mutator MutT protein homolog yvcI][GN:yvcI] [CL:mutT domain homology] [OR:Bacillus subtilis] 121 SPX19141914 4575 172 516 206 7.90E-37 [LN:F72234] [AC:F72234] [PN:transcriptionregulator, biotin repressor family] [GN:TM1602] [OR:Thermotoga maritima]116 SPX1915 1915 4576 194 582 NO-HIT 6 SPX1916 1916 4577 167 501 814.70E-09 [GI:806536] [LN:BAMALAMYA] [AC:Z22520] [PN:membrane protein][OR:Bacillus acidopullulyticus] 92 SPX1917 1917 4578 184 552 4652.50E-59 [LN:DFP_STRMU] [AC:Q54433] [GN:DFP] [OR:Streptococcus mutans][DE:DNA/PANTOTHENATE METABOLISM FLAVOPROTEIN HOMOLOG (FRAGMENT)][SP:Q54433] 138 SPX1918 1918 4579 253 759 120 2.90E-19 [LN:D69029][AC:D69029] [PN:pantothenate metabolism flavoprotein dfp homologMTH1216:probable aspartate 1-decarboxylase activase] [GN:MTH1216][CL:pantothenate metabolism flavoprotein dfp] [OR:Methanobacteriumthermoautotrophicum] 230 SPX1919 1919 4580 181 543 NO-HIT 6 SPX1920 19204581 557 1671 2475 0 [LN:FTHS_STRMU] [AC:Q59925:Q59926] [GN:FHS][OR:Streptococcus mutans] [EC:6.3.4.3] [DE:SYNTHETASE) (FHS) (FTHFS)][SP:Q59925:Q59926] 132 SPX1921 1921 4582 80 240 145 9.20E-16 [LN:T30285][AC:T30285] [PN:hypothetical protein] [OR:Streptococcus pneumoniae] 79SPX1922 1922 4583 392 1176 989 4.20E-132 [GI:6782414] [LN:SPN271596][AC:AJ271596] [PN:A/G specific adenine glycosylase] [GN:mutY][FN:antimutator prevents C to A transversions] [OR:Streptococcuspneumoniae] 166 SPX1923 1923 4584 235 705 1194 9.00E-161 [GI:5830523][LN:SPAJ6392] [AC:AJ006392] [PN:response regulator] [GN:rr02][OR:Streptococcus pneumoniae] 104 SPX1924 1924 4585 452 1356 2249 0[GI:5830524] [LN:SPAJ6392] [AC:AJ006392] [PN:histidine kinase] [GN:hk02][OR:Streptococcus pneumoniae] 102 SPX1925 1925 4586 270 810 13795.30E-185 [GI:6689278] [LN:SPN012049] [AC:AJ012049] [PN:VicX protein][GN:vicX] [FN:unknown] [OR:Streptococcus pneumoniae] 112 SPX1926 19264587 81 243 NO-HIT 6 SPX1927 1927 4588 88 264 93 1.90E-06 [LN:D70886][AC:D70886] [PN:hypothetical protein Rv2866] [GN:Rv2866][OR:Mycobacterium tuberculosis] 100 SPX1928 1928 4589 258 774 1623.00E-20 [LN:C72692] [AC:C72692] [PN:probable potassium channel APE0955][GN:APE0955] [OR:Aeropyrum pernix] 98 SPX1929 1929 4590 170 510 NO-HIT 6SPX1930 1930 4591 333 999 1652 9.40E-223 [GI:2275101] [LN:SPR6LDH][AC:AJ000336] [PN:L-lactate dehydrogenase] [GN:ldh] [FN:conversion ofpyruvate to lactate] [OR:Streptococcus pneumoniae] 146 SPX1931 1931 4592316 948 1617 3.30E-219 [LN:GYRA_STRPN] [AC:P72524:Q54716:P72536][GN:GYRA] [OR:Streptococcus pneumoniae] [EC:5.99.1.3] [DE:DNA GYRASESUBUNIT A,] [SP:P72524:Q54716:P72536] 150 SPX1932 1932 4593 119 357 2147.70E-24 [LN:GYRA_STRPN] [AC:P72524:Q54716:P72536] [GN:GYRA][OR:Streptococcus pneumoniae] [EC:5.99.1.3] [DE:DNA GYRASE SUBUNIT A,][SP:P72524:Q54716:P72536] 150 SPX1933 1933 4594 507 1521 2300 0[GI:4138535] [LN:SPN5815] [AC:AJ005815] [PN:DNA gyrase subunit A][GN:gyrA] [OR:Streptococcus pneumoniae] 105 SPX1934 1934 4595 248 744299 5.50E-36 [GI:488339] [LN:SYNGIP3124] [AC:M77279] [PN:alpha-amylase][OR:unidentified cloning vector] [SR:Cloning vector (sub_species Cloningvector pGIP3124) DNA] 153 SPX1935 1935 4596 266 798 184 6.20E-26[GI:4433636] [LN:AF029224] [AC:AF029224:AF029225] [PN:NirC] [GN:nirC][FN:putative nitrite transporter] [OR:Staphylococcus carnosus] 132SPX1936 1936 4597 372 1116 426 6.30E-115 [LN:T44655] [AC:T44655][PN:O-acetylhomoserine (thiol)-lyase, [imported]:O-acetylhomoserinesulfhydrylase] [CL:O-succinylhomoserine (thiol)-lyase] [OR:Leptospirameyeri] [EC:4.2.99.10] 186 SPX1937 1937 4598 425 1275 101 4.30E-18[GI:6899348] [LN:AE002133] [AC:AE002133:AF222894] [PN:conservedhypothetical] [GN:UU367] [OR:Ureaplasma urealyticum] 116 SPX1938 19384599 293 879 661 5.10E-86 [LN:TRUB_BACSU] [AC:P32732] [GN:TRUB][OR:Bacillus subtilis] [EC:4.2.1.70] [DE:HYDROLYASE)] [SP:P32732] 103SPX1939 1939 4600 101 303 NO-HIT 6 SPX1940 1940 4601 239 717 7073.50E-93 [LN:G69728] [AC:G69728] [PN:uridine kinase udk] [GN:udk][CL:uridine kinase] [OR:Bacillus subtilis] 99 SPX1941 1941 4602 447 1341633 1.60E-115 [LN:EX7L_BACSU] [AC:P54521] [GN:YQIB] [OR:Bacillussubtilis] [EC:3.1.11.6] [DE:VII LARGE SUBUNIT)] [SP:P54521] 110 SPX19421942 4603 71 213 113 3.50E-10 [LN:EX7S_ECOLI] [AC:P22938] [GN:XSEB][OR:Escherichia coli] [EC:3.1.11.6] [DE:SMALL SUBUNIT)] [SP:P22938] 105SPX1943 1943 4604 292 876 535 1.30E-78 [LN:ISPA_MICLU] [AC:O66126][GN:FPS] [OR:Micrococcus luteus] [SR:,Micrococcus lysodeikticus][EC:2.5.1.10] [DE:(FPP SYNTHASE)] [SP:O66126] 140 SPX1944 1944 4605 246738 353 1.20E-79 [LN:YQXC_BACSU] [AC:P19672] [GN:YQXC:YQIF] [OR:Bacillussubtilis] [DE:HYPOTHETICAL 29.7 KD PROTEIN IN FOLD-AHRC INTERGENICREGION] [SP:P19672] 142 SPX1945 1945 4606 144 432 182 4.10E-26[GI:4127534] [LN:BSAJ10954] [AC:AJ010954] [PN:arginine repressor][GN:argR] [FN:ADN binding protein] [OR:Bacillus stearothermophilus] 133SPX1946 1946 4607 298 894 317 4.20E-76 [LN:RECN_BACSU][AC:P17894:P19671] [GN:RECN] [OR:Bacillus subtilis] [DE:DNA REPAIRPROTEIN RECN (RECOMBINATION PROTEIN N)] [SP:P17894:P19671] 141 SPX19471947 4608 261 783 395 3.20E-68 [LN:RECN_BACSU] [AC:P17894:P19671][GN:RECN] [OR:Bacillus subtilis] [DE:DNA REPAIR PROTEIN RECN(RECOMBINATION PROTEIN N)] [SP:P17894:P19671] 141 SPX1948 1948 4609 243729 97 4.90E-15 [GI:2352096] [LN:U97022] [AC:U97022][OR:Fervidobacterium islandicum] 69 SPX1949 1949 4610 345 1035 12849.40E-173 [LN:LEPA_BACSU] [AC:P37949] [GN:LEPA] [OR:Bacillus subtilis][DE:GTP-BINDING PROTEIN LEPA] [SP:P37949] 102 SPX1950 1950 4611 304 9121158 1.80E-156 [LN:LEPA_BACSU] [AC:P37949] [GN:LEPA] [OR:Bacillussubtilis] [DE:GTP-BINDING PROTEIN LEPA] [SP:P37949] 102 SPX1951 19514612 111 333 95 7.80E-05 [LN:T04991] [AC:T04991] [PN:hypotheticalprotein T16L1.230] [OR:Arabidopsis thaliana] [SR:, mouse-ear cress] 110SPX1952 1952 4613 112 336 294 3.40E-35 [LN:T30285] [AC:T30285][PN:hypothetical protein] [OR:Streptococcus pneumoniae] 79 SPX1953 19534614 96 288 NO-HIT 6 SPX1954 1954 4615 230 690 70 3.10E-05 [LN:G75468][AC:G75468] [PN:hypothetical protein] [GN:DR0857] [OR:Deinococcusradiodurans] 90 SPX1955 1955 4616 60 180 NO-HIT 6 SPX1956 1956 4617 82246 NO-HIT 6 SPX1957 1957 4618 70 210 NO-HIT 6 SPX1958 1958 4619 68 204138 3.20E-14 [LN:LAFX_LACJO] [AC:Q48509] [GN:LAFX] [OR:Lactobacillusjohnsonii] [DE:BACTERIOCIN LACTACIN F, SUBUNIT LAFX PRECURSOR][SP:Q48509] 132 SPX1959 1959 4620 85 255 114 8.90E-21 [GI:5441255][LN:AB029612] [AC:AB029612] [PN:gassericin T1] [GN:gatA][OR:Lactobacillus gasseri] [SR:actobacillus gasseri (strain:SBT2055)DNA] 144 SPX1960 1960 4621 56 168 79 0.00078 [GI:6751696][LN:ATAC018908] [AC:AC018908] [GN:T7P1.21] [OR:Arabidopsis thaliana][SR:thale cress] 98 SPX1961 1961 4622 182 546 379 2.90E-48 [LN:S52544][AC:S52544] [PN:ISL2 protein] [OR:Lactobacillus helveticus] 71 SPX19621962 4623 133 399 364 8.90E-50 [LN:S52544] [AC:S52544] [PN:ISL2 protein][OR:Lactobacillus helveticus] 71 SPX1963 1963 4624 55 165 NO-HIT 6SPX1964 1964 4625 68 204 NO-HIT 6 SPX1965 1965 4626 69 207 NO-HIT 6SPX1966 1966 4627 68 204 55 0.00018 [GI:6457574] [LN:AF200347][AC:AF200347] [PN:lactocin 705 beta-subunit precursor] [OR:Lactobacilluscasei] 106 SPX1967 1967 4628 73 219 NO-HIT 6 SPX1968 1968 4629 718 21542269 0 [LN:COMA_STRPN] [AC:Q03727] [GN:COMA] [OR:Streptococcuspneumoniae] [DE:TRANSPORT ATP-BINDING PROTEIN COMA] [SP:Q03727] 119SPX1969 1969 4630 83 249 80 0.00032 [LN:G72510] [AC:G72510][PN:hypothetical protein APE2061] [GN:APE2061] [OR:Aeropyrum pernix] 92SPX1970 1970 4631 454 1362 697 7.40E-90 [GI:1698422] [LN:SGU40139][AC:U40139] [PN:ComB] [GN:comB] [OR:Streptococcus gordonii][SR:Streptococcus gordonii strain=Challis] 129 SPX1971 1971 4632 67 201NO-HIT 6 SPX1972 1972 4633 110 330 NO-HIT 6 SPX1973 1973 4634 447 13412062 1.10E-288 [GI:5830551] [LN:SPAJ6401] [AC:AJ006401] [PN:histidinekinase] [GN:hk13] [OR:Streptococcus pneumoniae] 102 SPX1974 1974 4635215 645 972 3.30E-133 [GI:5830550] [LN:SPAJ6401] [AC:AJ006401][PN:response regulator] [GN:rr13] [OR:Streptococcus pneumoniae] 104SPX1975 1975 4636 61 183 239 4.40E-28 [GI:5830550] [LN:SPAJ6401][AC:AJ006401] [PN:response regulator] [GN:rr13] [OR:Streptococcuspneumoniae] 104 SPX1976 1976 4637 113 339 69 0.000063 [GI:1495671][LN:LPATOVGNS] [AC:X94434] [PN:response regulator PlnC] [GN:plnC][OR:Lactobacillus plantarum] 107 SPX1977 1977 4638 110 330 NO-HIT 6SPX1978 1978 4639 69 207 NO-HIT 6 SPX1979 1979 4640 324 972 150 4.10E-24[LN:ECSB_BACSU] [AC:P55340] [GN:ECSB:PRST] [OR:Bacillus subtilis][DE:PROTEIN ECSB] [SP:P55340] 95 SPX1980 1980 4641 74 222 NO-HIT 6SPX1981 1981 4642 115 345 333 4.00E-42 [LN:ECSA_BACSU] [AC:P55339][GN:ECSA:PRST] [OR:Bacillus subtilis] [DE:ABC-TYPE TRANSPORTERATP-BINDING PROTEIN ECSA] [SP:P55339] 128 SPX1982 1982 4643 126 378 3912.60E-49 [LN:ECSA_BACSU] [AC:P55339] [GN:ECSA:PRST] [OR:Bacillussubtilis] [DE:ABC-TYPE TRANSPORTER ATP-BINDING PROTEIN ECSA] [SP:P55339]128 SPX1983 1983 4644 137 411 334 8.80E-42 [LN:HIT_BACSU] [AC:O07513][GN:HIT] [OR:Bacillus subtilis] [DE:HIT PROTEIN] [SP:O07513] 87 SPX19841984 4645 96 288 NO-HIT 6 SPX1985 1985 4646 85 255 NO-HIT 6 SPX1986 19864647 379 1137 1885 4.90E-254 [LN:DNAJ_STRPN] [AC:P95830] [GN:DNAJ][OR:Streptococcus pneumoniae] [DE:DNAJ PROTEIN (FRAGMENT)] [SP:P95830]108 SPX1987 1987 4648 47 141 125 7.20E-10 [GI:5305335] [LN:AF071081][AC:AF071081] [PN:proline-rich mucin homolog] [OR:Mycobacteriumtuberculosis] 104 SPX1988 1988 4649 119 357 NO-HIT 6 SPX1989 1989 465086 258 NO-HIT 6 SPX1990 1990 4651 608 1824 3008 0 [LN:DNAK_STRPN][AC:P95829:O66035] [GN:DNAK] [OR:Streptococcus pneumoniae] [DE:DNAKPROTEIN (HEAT SHOCK PROTEIN 70) (HSP70)] [SP:P95829:O66035] 143 SPX19911991 4652 120 360 NO-HIT 6 SPX1992 1992 4653 218 654 NO-HIT 6 SPX19931993 4654 183 549 346 3.60E-74 [LN:GRPE_LACLA] [AC:P42369] [GN:GRPE][OR:Lactococcus lactis] [SR:,subsplactis:Streptococcus lactis] [DE:GRPEPROTEIN] [SP:P42369] 132 SPX1994 1994 4655 356 1068 1712 6.90E-235[GI:4566769] [LN:AF117740] [AC:AF117740] [PN:heat shock transcriptionrepressor HrcA] [GN:hrcA] [OR:Streptococcus pneumoniae] 125 SPX1995 19954656 170 510 NO-HIT 6 SPX1996 1996 4657 778 2334 570 9.20E-238[LN:I41291] [AC:I41291] [PN:EcoA type I restriction-modification enzymeR subunit] [OR:Escherichia coli] 104 SPX1997 1997 4658 488 1464 8461.80E-144 [LN:I41293] [AC:I41293] [PN:EcoE type I restrictionmodification enzyme M subunit] [CL:site-specific methyltransferase(adenine-specific) EcoK] [OR:Escherichia coli] 165 SPX1998 1998 4659 5171551 323 1.60E-37 [GI:6899439] [LN:AE002141] [AC:AE002141:AF222894][PN:type I restriction enzyme S protein (fragment)] [GN:hsdS-5][OR:Ureaplasma urealyticum] 141 SPX1999 1999 4660 430 1290 328 1.40E-38[GI:6899439] [LN:AE002141] [AC:AE002141:AF222894] [PN:type I restrictionenzyme S protein (fragment)] [GN:hsdS-5] [OR:Ureaplasma urealyticum] 141SPX2000 2000 4661 74 222 NO-HIT 6 SPX2001 2001 4662 449 1347 12656.40E-246 [GI:1815634] [LN:SAU61271] [AC:U61271] [PN:glutaminesynthetase type 1] [GN:glnA] [OR:Streptococcus agalactiae] 111 SPX20022002 4663 119 357 244 7.30E-29 [LN:GLNR_BACCE] [AC:P19083] [GN:GLNR][OR:Bacillus cereus] [DE:REGULATORY PROTEIN GLNR] [SP:P19083] 99 SPX20032003 4664 176 528 100 1.00E-06 [LN:H69815] [AC:H69815] [PN:hypotheticalprotein ygaE] [GN:ygaE] [OR:Bacillus subtilis] 87 SPX2004 2004 4665 126378 137 1.10E-11 [LN:S72776] [AC:S72776] [PN:B1496_F1_41 protein][OR:Mycobacterium leprae] 74 SPX2005 2005 4666 399 1197 622 6.20E-166[GI:4490614] [LN:SAU133520] [AC:AJ133520] [PN:phosphoglycerate kinase][GN:pgk] [OR:Staphylococcus aureus] 106 SPX2006 2006 4667 1647 4941 2073.10E-63 [GI:4204919] [LN:APU59168] [AC:U59168][PN:endo-beta-N-acetylglucosaminidase] [OR:Arthrobacter protophormiae]109 SPX2007 2007 4668 171 513 NO-HIT 6 SPX2008 2008 4669 544 1632 2493.20E-57 [LN:H71283] [AC:H71283] [PN:conserved hypothetical integralmembrane protein TP0771] [GN:TP0771] [OR:Treponema pallidum subsp.pallidum] [SR:, syphilis spirochete] 165 SPX2009 2009 4670 536 1608 23030 [LN:LAJ10153] [AC:AJ010153] [PN:CTP synthetase] [GN:pyrG][OR:Lactococcus lactis subsp. cremoris] 97 SPX2010 2010 4671 44 132 1376.60E-15 [LN:T30285] [AC:T30285] [PN:hypothetical protein][OR:Streptococcus pneumoniae] 79 SPX2011 2011 4672 196 588 169 1.20E-25[LN:RPOE_BACSU] [AC:P12464] [GN:RPOE] [OR:Bacillus subtilis][EC:2.7.7.6] [DE:DNA-DIRECTED RNA POLYMERASE DELTA SUBUNIT,] [SP:P12464]135 SPX2012 2012 4673 150 450 NO-HIT 6 SPX2013 2013 4674 130 390 NO-HIT6 SPX2014 2014 4675 217 651 179 5.00E-19 [LN:S32217] [AC:S32217][PN:hypothetical protein 2] [OR:Bacillus megaterium] 76 SPX2015 20154676 188 564 258 3.20E-32 [LN:YPAA_BACSU] [AC:P50726] [GN:YPAA][OR:Bacillus subtilis] [DE:HYPOTHETICAL 20.5 KD PROTEIN IN SERA-FERINTERGENIC REGION] [SP:P50726] 136 SPX2016 2016 4677 73 219 NO-HIT 6SPX2017 2017 4678 156 468 243 6.60E-44 [GI:1381681] [LN:BSU58864][AC:U58864] [PN:CspR] [GN:cspR] [OR:Bacillus subtilis] [SR:Bacillussubtilis strain=JH642] 117 SPX2018 2018 4679 277 831 83 4.70E-12[LN:Y181_MYCPN] [AC:Q50292] [OR:Mycoplasma pneumoniae] [DE:HYPOTHETICALPROTEIN MG181 HOMOLOG (GT9_ORF434)] [SP:Q50292] 119 SPX2019 2019 4680416 1248 343 1.40E-50 [LN:G64435] [AC:G64435] [PN:cobalt transportATP-binding protein O homolog] [CL:unassigned ATP-binding cassetteproteins:ATP-binding cassette homology] [OR:Methanococcus jannaschii]181 SPX2020 2020 4681 128 384 230 1.10E-25 [LN:G71192] [AC:G71192][PN:probable cobalt transport ATP-binding protein] [GN:PH1815][CL:unassigned ATP-binding cassette proteins:ATP-binding cassettehomology] [OR:Pyrococcus horikoshii] 189 SPX2021 2021 4682 71 213 NO-HIT6 SPX2022 2022 4683 86 258 NO-HIT 6 SPX2023 2023 4684 183 549 4941.60E-73 [GI:6165407] [LN:LLA012388] [AC:AJ012388] [PN:hypotheticalprotein] [OR:Lactococcus lactis] 91 SPX2024 2024 4685 292 876 5462.00E-98 [LN:E64608] [AC:E64608] [PN:conserved hypothetical proteinHP0709] [OR:Helicobacter pylori] 91 SPX2025 2025 4686 450 1350 2581.20E-60 [LN:F69354] [AC:F69354] [PN:TRK potassium uptake system protein(trkA-2) homolog] [CL:Methanococcus jannaschii TRK system potassiumuptake protein A] [OR:Archaeoglobus fulgidus] 177 SPX2026 2026 4687 4791437 232 7.20E-73 [LN:G69354] [AC:G69354] [PN:TRK potassium uptakesystem protein (trkH) homolog] [CL:potassium uptake protein trkG][OR:Archaeoglobus fulgidus] 142 SPX2027 2027 4688 560 1680 777 1.20E-171[LN:PTLB_STRMU] [AC:P50976] [GN:LACE] [OR:Streptococcus mutans][EC:2.7.1.69] [DE:(EC 2.7.1.69) (EII-LAC)] [SP:P50976] 118 SPX2028 20284689 471 1413 643 5.80E-164 [GI:153755] [LN:STRPBGSL] [AC:M19454][OR:Lactococcus lactis subsp. cremoris] [SR:S.lactis (strain Z268) DNA,clone X25] 122 SPX2029 2029 4690 65 195 NO-HIT 6 SPX2030 2030 4691 115345 298 8.20E-37 [LN:PTLA_LACCA] [AC:P11502] [GN:LACF] [OR:Lactobacilluscasei] [EC:2.7.1.69] [DE:(EC 2.7.1.69) (EIII-LAC)] [SP:P11502] 118SPX2031 2031 4692 647 1941 NO-HIT 6 SPX2032 2032 4693 441 1323 3951.00E-89 [LN:PTCC_BACST] [AC:Q45400] [GN:CELB] [OR:Bacillusstearothermophilus] [DE:PERMEASE IIC COMPONENT) (PHOSPHOTRANSFERASEENZYME II, C COMPONENT)] [SP:Q45400] 157 SPX2033 2033 4694 408 1224 1472.50E-21 [LN:XYLR_BACSU] [AC:P16557] [GN:XYLR] [OR:Bacillus subtilis][DE:XYLOSE REPRESSOR] [SP:P16557] 94 SPX2034 2034 4695 73 219 NO-HIT 6SPX2035 2035 4696 58 174 NO-HIT 6 SPX2036 2036 4697 62 186 NO-HIT 6SPX2037 2037 4698 95 285 167 2.40E-18 [GI:2707293] [LN:AF036720][AC:AF036720] [PN:unknown] [OR:Lactococcus lactis] 77 SPX2038 2038 4699173 519 879 6.50E-119 [GI:663278] [LN:STRCOMAA] [AC:M36180:L15190][PN:transposase] [OR:Streptococcus pneumoniae] [SR:Streptococcuspneumoniae (strain RX1) DNA] 138 SPX2039 2039 4700 256 768 12351.10E-172 [GI:663279] [LN:STRCOMAA] [AC:M36180:L15190] [PN:transposase][OR:Streptococcus pneumoniae] [SR:Streptococcus pneumoniae (strain RX1)DNA] 138 SPX2040 2040 4701 421 1263 948 4.80E-188 [GI:2687821][LN:STIS1193] [AC:Y13713] [PN:transposase] [OR:Streptococcusthermophilus] 87 SPX2041 2041 4702 86 258 149 1.10E-14 [GI:2198546][LN:SPCPS14E] [AC:X85787] [GN:tasA] [OR:Streptococcus pneumoniae] 78SPX2042 2042 4703 775 2325 3774 0 [GI:3168596] [LN:AB014686][AC:AB014686] [PN:pyruvate formate-lyase] [GN:pfl] [OR:Streptococcusbovis] [SR:Streptococcus bovis (strain:JB-1) DNA] 145 SPX2043 2043 470492 276 133 7.70E-20 [LN:T30285] [AC:T30285] [PN:hypothetical protein][OR:Streptococcus pneumoniae] 79 SPX2044 2044 4705 78 234 NO-HIT 6SPX2045 2045 4706 357 1071 491 2.70E-83 [GI:7380303] [LN:NMA5Z2491][AC:AL162756:AL157959] [PN:impB/mucB/samB family protein] [GN:NMA1661][OR:Neisseria meningitidis] 126 SPX2046 2046 4707 63 189 NO-HIT 6SPX2047 2047 4708 282 846 289 6.60E-52 [GI:5739401] [LN:AF169967][AC:AF169967] [PN:BacA] [GN:bacA] [OR:Flavobacterium johnsoniae] 91SPX2048 2048 4709 217 651 139 3.00E-12 [LN:YIS1_STRCO] [AC:P19780][GN:SC3C8.10] [OR:Streptomyces coelicolor] [DE:INSERTION ELEMENT IS110HYPOTHETICAL 43.6 KD PROTEIN] [SP:P19780] 140 SPX2049 2049 4710 62 186NO-HIT 6 SPX2050 2050 4711 631 1893 95 3.20E-08 [LN:H64496] [AC:H64496][PN:hypothetical protein MJ1577] [OR:Methanococcus jannaschii] 86SPX2051 2051 4712 522 1566 331 9.10E-53 [LN:A72357] [AC:A72357][PN:amino acid ABC transporter, permease protein] [GN:TM0592][CL:histidine permease protein M] [OR:Thermotoga maritima] 146 SPX20522052 4713 247 741 388 9.60E-89 [LN:F81363] [AC:F81363] [PN:probableglutamine transport ATP-binding protein Cj0902 [imported]][GN:glnQ:Cj0902] [OR:Campylobacter jejuni] 138 SPX2053 2053 4714 72 216NO-HIT 6 SPX2054 2054 4715 77 231 NO-HIT 6 SPX2055 2055 4716 66 198 2541.20E-29 [GI:2804700] [LN:AF030361] [AC:AF030361] [PN:transposase][OR:Streptococcus pneumoniae] 87 SPX2056 2056 4717 128 384 511 2.70E-66[GI:5739312] [LN:AF161700] [AC:AF161700] [PN:ComX1] [GN:comX1][FN:transcriptional regulator of] [OR:Streptococcus pneumoniae] 126SPX2057 2057 4718 184 552 442 1.30E-63 [LN:NUSG_BACSU] [AC:Q06795][GN:NUSG] [OR:Bacillus subtilis] [DE:TRANSCRIPTION ANTITERMINATIONPROTEIN NUSG] [SP:Q06795] 120 SPX2058 2058 4719 59 177 NO-HIT 6 SPX20592059 4720 732 2196 3714 0 [GI:6165960] [LN:AF101780] [AC:AF101780][PN:penicillin-binding protein 2a] [GN:pbp2a] [OR:Streptococcuspneumoniae] 116 SPX2060 2060 4721 292 876 229 4.10E-34 [LN:YHCT_BACSU][AC:P54604] [GN:YHCT] [OR:Bacillus subtilis] [DE:HYPOTHETICAL 33.7 KDPROTEIN IN CSPB-GLPP INTERGENIC REGION] [SP:P54604] 137 SPX2061 20614722 360 1080 1061 2.30E-215 [LN:A42963] [AC:A42963:B42963:JH0750][PN:glyceraldehyde-3-phosphate dehydrogenase,:plasmin receptor][CL:glyceraldehyde-3-phosphate dehydrogenase] [OR:Streptococcus sp.][EC:1.2.1.12] 186 SPX2062 2062 4723 92 276 NO-HIT 6 SPX2063 2063 4724317 951 124 1.80E-15 [LN:Y797_METJA] [AC:Q58207] [GN:MJ0797][OR:Methanococcus jannaschii] [DE:HYPOTHETICAL PROTEIN MJ0797][SP:Q58207] 114 SPX2064 2064 4725 113 339 552 2.20E-73 [GI:5019553][LN:SPN239004] [AC:AJ239004] [PN:putative transposase] [OR:Streptococcuspneumoniae] 97 SPX2065 2065 4726 87 261 NO-HIT 6 SPX2066 2066 4727 116348 577 5.80E-76 [GI:4200438] [LN:AF026471] [AC:AF026471] [PN:putativetransposase] [OR:Streptococcus pneumoniae] 96 SPX2067 2067 4728 300 900482 2.20E-71 [LN:B70375] [AC:B70375] [PN:quinolinate phosphoribosyltransferase] [GN:nadC] [CL:nicotinate-nucleotide pyrophosphorylase(carboxylating)] [OR:Aquifex aeolicus] 160 SPX2068 2068 4729 437 1311448 2.70E-105 [LN:C81402] [AC:C81402] [PN:probable integral membraneprotein Cj0555 [imported]] [GN:Cj0555] [OR:Campylobacter jejuni] 119SPX2069 2069 4730 62 186 NO-HIT 6 SPX2070 2070 4731 65 195 111 7.10E-09[LN:H81018] [AC:H81018] [PN:iron(III) ABC transporter, ATP-bindingprotein NMB1993 [imported]] [GN:NMB1993] [OR:Neisseria meningitidis] 137SPX2071 2071 4732 243 729 352 3.20E-72 [GI:4512387] [LN:AB011838][AC:AB011838] [GN:ydhQ] [OR:Bacillus halodurans] [SR:Bacillus halodurans(strain:C-125) DNA, clone_lib:lambda no.] 143 SPX2072 2072 4733 470 1410808 8.30E-181 [LN:D69785] [AC:D69785] [PN:beta-glucosidase homolog ydhP][GN:ydhP] [CL:Agrobacterium beta-glucosidase] [OR:Bacillus subtilis] 127SPX2073 2073 4734 432 1296 330 7.00E-64 [LN:PTCC_BACSU] [AC:P46317][GN:CELB:LICC] [OR:Bacillus subtilis] [DE:PERMEASE IIC COMPONENT)(PHOSPHOTRANSFERASE ENZYME II, C COMPONENT)] [SP:P46317] 152 SPX20742074 4735 129 387 NO-HIT 6 SPX2075 2075 4736 103 309 191 2.70E-30[LN:PTCB_BACST] [AC:Q45399] [GN:CELA] [OR:Bacillus stearothermophilus][EC:2.7.1.69] [DE:(EC 2.7.1.69)] [SP:Q45399] 115 SPX2076 2076 4737 103309 210 6.00E-24 [LN:PTCA_BACSU] [AC:P46319] [GN:CELC:LICA] [OR:Bacillussubtilis] [EC:2.7.1.69] [DE:(EC 2.7.1.69) (EIII-CEL)] [SP:P46319] 121SPX2077 2077 4738 75 225 NO-HIT 6 SPX2078 2078 4739 891 2673 2272 0[LN:ADH2_ENTHI] [AC:Q24803:Q27649] [GN:ADH2] [OR:Entamoeba histolytica][EC:1.1.1.1:1.2.1.10] [DE:(EC 1.1.1.1) (ADH); ALCETALDEHYDEDEHYDROGENASE, (ACDH)]] [SP:Q24803:Q27649] 176 SPX2079 2079 4740 137 411168 4.10E-18 [GI:6010051] [LN:ECA270205] [AC:AJ270205] [PN:putativephosphatidylinositol-4-phosphate] [OR:Entodinium caudatum] 113 SPX20802080 4741 143 429 91 7.10E-26 [LN:E69808] [AC:E69808][PN:protein-tyrosine phosphatase homolog yfkJ] [GN:yfkJ][CL:protein-tyrosine-phosphatase, low molecular weight] [OR:Bacillussubtilis] 161 SPX2081 2081 4742 100 300 177 9.30E-20 [GI:1402532][LN:D78257] [AC:D78257] [PN:ORF11] [GN:orf11] [OR:Enterococcus faecalis][SR:Enterococcus faecalis plasmid:pYI17 DNA] 130 SPX2082 2082 4743 6591977 1671 0 [LN:TKT_STRPN] [AC:P22976] [GN:RECP] [OR:Streptococcuspneumoniae] [EC:2.2.1.1] [DE:PROBABLE TRANSKETOLASE, (TK)] [SP:P22976]127 SPX2083 2083 4744 81 243 171 1.00E-17 [LN:TKT_STRPN] [AC:P22976][GN:RECP] [OR:Streptococcus pneumoniae] [EC:2.2.1.1] [DE:PROBABLETRANSKETOLASE, (TK)] [SP:P22976] 127 SPX2084 2084 4745 102 306 2771.50E-33 [LN:TKT_STRPN] [AC:P22976] [GN:RECP] [OR:Streptococcuspneumoniae] [EC:2.2.1.1] [DE:PROBABLE TRANSKETOLASE, (TK)] [SP:P22976]127 SPX2085 2085 4746 245 735 546 8.30E-96 [LN:YJFR_ECOLI] [AC:P39300][GN:YJFR] [OR:Escherichia coli] [DE:HYPOTHETICAL 40.1 KD PROTEIN INAIDB-SGAT INTERGENIC REGION] [SP:P39300] 136 SPX2086 2086 4747 136 408430 3.30E-54 [LN:YJFR_ECOLI] [AC:P39300] [GN:YJFR] [OR:Escherichia coli][DE:HYPOTHETICAL 40.1 KD PROTEIN IN AIDB-SGAT INTERGENIC REGION][SP:P39300] 136 SPX2087 2087 4748 558 1674 178 6.30E-20 [GI:4512373][LN:AB011837] [AC:AB011837] [GN:yjdC] [OR:Bacillus halodurans][SR:Bacillus halodurans (strain:C-125) DNA, clone_lib:lambda no.9] 144SPX2088 2088 4749 235 705 489 3.20E-93 [GI:5616307] [LN:AF160811][AC:AF160811] [PN:L-ribulose 5-phosphate 4-epimerase] [GN:araD][OR:Bacillus stearothermophilus] 123 SPX2089 2089 4750 288 864 7773.20E-106 [LN:SGBU_HAEIN] [AC:P44990] [GN:SGBU:HI1026] [OR:Haemophilusinfluenzae] [EC:5.-.-.-] [DE:PUTATIVE HEXULOSE-6-PHOSPHATE ISOMERASE,(HUMPI)] [SP:P44990] 153 SPX2090 2090 4751 222 666 349 1.00E-70[LN:SGAH_ECOLI] [AC:P39304] [GN:SGAH] [OR:Escherichia coli] [EC:4.1.2.-][DE:3-HEXULOSE 6-PHOSPHATE FORMALDEHYDE LYASE)] [SP:P39304] 132 SPX20912091 4752 162 486 266 1.10E-45 [LN:PTXA_ECOLI] [AC:P39303] [GN:SGAA][OR:Escherichia coli] [EC:2.7.1.69] [DE:(EC 2.7.1.69)] [SP:P39303] 104SPX2092 2092 4753 94 282 111 6.80E-22 [LN:PTXB_ECOLI] [AC:P39302][GN:SGAB] [OR:Escherichia coli] [EC:2.7.1.69] [DE:(EC 2.7.1.69)][SP:P39302] 104 SPX2093 2093 4754 509 1527 275 5.90E-99 [LN:SGAT_ECOLI][AC:P39301] [GN:SGAT] [OR:Escherichia coli] [DE:PUTATIVE TRANSPORTPROTEIN SGAT] [SP:P39301] 108 SPX2094 2094 4755 208 624 210 1.10E-38[GI:6681651] [LN:AB016077] [AC:AB016077] [PN:sakacin A productionresponse regulator] [GN:sapR] [OR:Streptococcus mutans][SR:Streptococcus mutans (strain:MT8148) DNA, clone:pYT570] 183 SPX20952095 4756 329 987 145 1.90E-24 [LN:JAG_BACSU] [AC:Q01620] [GN:JAG][OR:Bacillus subtilis] [DE:JAG PROTEIN (SPOIIIJ ASSOCIATED PROTEIN)][SP:Q01620] 116 SPX2096 2096 4757 277 831 357 1.00E-51 [LN:SP3J_BACSU][AC:Q01625] [GN:SPOIIIJ] [OR:Bacillus subtilis] [DE:STAGE IIISPORULATION PROTEIN J PRECURSOR] [SP:Q01625] 122 SPX2097 2097 4758 124372 173 3.10E-31 [GI:5672645] [LN:AB013492] [AC:AB013492] [GN:rnpA][OR:Bacillus halodurans] [SR:Bacillus halodurans (strain:C-125) DNA,clone:ALBAC001] 137 SPX2098 2098 4759 397 1191 822 1.30E-149[LN:ACKA_BACSU] [AC:P37877] [GN:ACKA] [OR:Bacillus subtilis][EC:2.7.2.1] [DE:ACETATE KINASE, (ACETOKINASE)] [SP:P37877] 122 SPX20992099 4760 318 954 297 4.70E-44 [LN:YTXK_BACSU] [AC:P37876] [GN:YTXK][OR:Bacillus subtilis] [DE:HYPOTHETICAL 37.4 KD PROTEIN IN ACKA-SSPAINTERGENIC REGION] [SP:P37876] 137 SPX2100 2100 4761 196 588 1322.90E-10 [LN:H70323] [AC:H70323] [PN:hypothetical protein aq_262][GN:aq_262] [OR:Aquifex aeolicus] 90 SPX2101 2101 4762 138 414 NO-HIT 6SPX2102 2102 4763 169 507 157 1.60E-30 [GI:3287181] [LN:LLC3107][AC:Y15043] [GN:orf150] [OR:Lactococcus lactis subsp. cremoris] 89SPX2103 2103 4764 101 303 123 9.50E-12 [GI:3287182] [LN:LLC3107][AC:Y15043] [PN:hypothetical protein] [GN:orf128] [OR:Lactococcus lactissubsp. cremoris] 115 SPX2104 2104 4765 135 405 626 3.00E-81 [GI:3211751][LN:AF052207] [AC:AF052207] [PN:competence protein] [GN:cglD][OR:Streptococcus pneumoniae] 104 SPX2105 2105 4766 109 327 512 5.80E-66[GI:3211750] [LN:AF052207] [AC:AF052207] [PN:competence protein][GN:cglC] [OR:Streptococcus pneumoniae] 104 SPX2106 2106 4767 348 10441440 3.30E-199 [GI:3211749] [LN:AF052207] [AC:AF052207] [PN:competenceprotein] [GN:cglB] [OR:Streptococcus pneumoniae] 104 SPX2107 2107 4768314 942 1592 4.30E-217 [GI:3211748] [LN:AF052207] [AC:AF052207][PN:competence protein] [GN:cglA] [OR:Streptococcus pneumoniae] 104SPX2108 2108 4769 124 372 468 9.20E-61 [GI:2058543] [LN:SGU81957][AC:U81957] [PN:putative DNA binding protein] [OR:Streptococcusgordonii] 100 SPX2109 2109 4770 353 1059 639 1.60E-125 [LN:T36961][AC:T36961] [PN:probable zinc-containing dehydrogenase] [GN:SCJ1.28c][CL:alcohol dehydrogenase:long-chain alcohol dehydrogenase homology][OR:Streptomyces coelicolor] 179 SPX2110 2110 4771 142 426 NO-HIT 6SPX2111 2111 4772 384 1152 819 3.90E-108 [GI:6683552] [LN:AB024532][AC:AB024532] [GN:SA8A11-1] [OR:Enterococcus seriolicida][SR:Enterococcus seriolicida DNA] 118 SPX2112 2112 4773 606 1818 1732.40E-27 [LN:C69975] [AC:C69975] [PN:acyltransferase homolog yrhL][GN:yrhL] [OR:Bacillus subtilis] 90 SPX2113 2113 4774 381 1143 14693.70E-200 [LN:TGT_BACSU] [AC:O32053] [GN:TGT] [OR:Bacillus subtilis][EC:2.4.2.29] [DE:TRANSGLYCOSYLASE) (GUANINE INSERTION ENZYME)][SP:O32053] 134 SPX2114 2114 4775 286 858 90 9.00E-05 [LN:S32215][AC:S32215] [PN:hypothetical protein 1] [OR:Bacillus megaterium] 76SPX2115 2115 4776 215 645 769 1.20E-104 [LN:PCP_STRPY] [AC:Q01328][GN:PCP] [OR:Streptococcus pyogenes] [EC:3.4.19.3] [DE:PEPTIDASE)(PYROGLUTAMYL-PEPTIDASE I) (PGP-I) (PYRASE)] [SP:Q01328] 149 SPX21162116 4777 90 270 NO-HIT 6 SPX2117 2117 4778 120 360 221 1.90E-43[LN:YTRP_LACLA] [AC:Q02009] [OR:Lactococcus lactis][SR:,subsplactis:Streptococcus lactis] [DE:HYPOTHETICAL 13.3 KD PROTEININ TRPE 5′REGION] [SP:Q02009] 155 SPX2118 2118 4779 142 426 163 3.50E-17[LN:D69783] [AC:D69783] [PN:transcription regulator MarR family homologydgJ] [GN:ydgJ] [CL:regulatory protein mprA] [OR:Bacillus subtilis] 139SPX2119 2119 4780 69 207 107 2.10E-10 [GI:1914870] [LN:SPZ82001][AC:Z82001] [PN:unknown] [OR:Streptococcus pneumoniae] 81 SPX2120 21204781 371 1113 382 8.00E-79 [GI:517204] [LN:SPU09352] [AC:U09352][OR:Streptococcus pyogenes] 65 SPX2121 2121 4782 207 621 153 7.60E-14[LN:A57362] [AC:A57362] [PN:gyrb protein] [GN:gyrb] [OR:Streptococcuspneumoniae] 81 SPX2122 2122 4783 427 1281 216 1.10E-45 [LN:H72331][AC:H72331] [PN:conserved hypothetical protein] [GN:TM0815][CL:conserved hypothetical protein HI1612] [OR:Thermotoga maritima] 139SPX2123 2123 4784 495 1485 412 4.80E-66 [LN:B64532] [AC:B64532][PN:threonine synthase] [CL:threonine synthase] [OR:Helicobacter pylori]96 SPX2124 2124 4785 426 1278 70 0.00014 [LN:T05142][AC:T05142:S60128:S45018] [PN:gamma-glutamylcysteine synthetase:proteinF7H19.290] [OR:Arabidopsis thaliana] [SR:, mouse-ear cress] [EC:6.3.2.2]158 SPX2125 2125 4786 59 177 100 1.30E-08 [LN:C64671] [AC:C64671][PN:hypothetical protein HP1211] [OR:Helicobacter pylori] 81 SPX21262126 4787 61 183 81 9.30E-05 [LN:E72688] [AC:E72688] [PN:hypotheticalprotein APE0925] [GN:APE0925] [CL:Aeropyrum pernix hypothetical proteinAPE0925] [OR:Aeropyrum pernix] 143 SPX2127 2127 4788 78 234 143 4.90E-15[LN:F71245] [AC:F71245] [PN:hypothetical protein PHS004] [GN:PHS004][OR:Pyrococcus horikoshii] 95 SPX2128 2128 4789 82 246 247 1.10E-29[LN:F81737] [AC:F81737] [PN:hypothetical protein TC0129 [imported]][GN:TC0129] [OR:Chlamydia muridarum:Chlamydia trachomatis MoPn] 131SPX2129 2129 4790 52 156 80 3.00E-05 [LN:D75542] [AC:D75542][PN:hypothetical protein] [GN:DR0254] [OR:Deinococcus radiodurans] 90SPX2130 2130 4791 105 315 NO-HIT 6 SPX2131 2131 4792 146 438 4861.80E-62 [GI:517210] [LN:SPU11799] [AC:U11799] [OR:Streptococcuspyogenes] 65 SPX2132 2132 4793 354 1062 824 6.40E-132 [GI:1915907][LN:LLPEPPGEN] [AC:Y08842] [PN:aminopeptidase P] [GN:pepP][OR:Lactococcus lactis] 95 SPX2133 2133 4794 944 2832 2029 0[LN:UVRA_BACSU] [AC:O34863] [GN:UVRA] [OR:Bacillus subtilis][DE:EXCINUCLEASE ABC SUBUNIT A] [SP:O34863] 104 SPX2134 2134 4795 315945 236 1.50E-26 [LN:A75272] [AC:A75272] [PN:probable transport protein][GN:DR2463] [CL:magnesium and cobalt transport protein] [OR:Deinococcusradiodurans] 140 SPX2135 2135 4796 68 204 NO-HIT 6 SPX2136 2136 4797 213639 NO-HIT 6 SPX2137 2137 4798 51 153 123 1.60E-12 [GI:1914870][LN:SPZ82001] [AC:Z82001] [PN:unknown] [OR:Streptococcus pneumoniae] 81SPX2138 2138 4799 344 1032 86 1.10E-19 [LN:E75325] [AC:E75325][PN:probable mccF protein] [GN:DR2000] [OR:Deinococcus radiodurans] 91SPX2139 2139 4800 226 678 66 3.80E-08 [GI:6470197] [LN:AF188935][AC:AF188935] [PN:pXO2-46] [OR:Bacillus anthracis] 77 SPX2140 2140 4801188 564 465 3.30E-63 [LN:3MGA_HAEIN] [AC:P44321] [GN:TAG:HI0654][OR:Haemophilus influenzae] [EC:3.2.2.20] [DE:GLYCOSIDASE) (TAG)][SP:P44321] 121 SPX2141 2141 4802 186 558 NO-HIT 6 SPX2142 2142 4803 198594 235 1.00E-38 [LN:RUVA_BACSU] [AC:O05392] [GN:RUVA] [OR:Bacillussubtilis] [DE:PROBABLE HOLLIDAY JUNCTION DNA HELICASE RUVA] [SP:O05392]122 SPX2143 2143 4804 70 210 NO-HIT 6 SPX2144 2144 4805 367 1101 8886.00E-128 [LN:RIBD_ACTPL] [AC:P50853] [GN:RIBD:RIBG] [OR:Actinobacilluspleuropneumoniae] [SR:,Haemophilus pleuropneumoniae] [EC:3.5.4.-][DE:RIBOFLAVIN-SPECIFIC DEAMINASE,] [SP:P50853] 177 SPX2145 2145 4806212 636 601 1.70E-81 [LN:RISA_ACTPL] [AC:P50854] [GN:RIBE:RIBB][OR:Actinobacillus pleuropneumoniae] [SR:,Haemophilus pleuropneumoniae][EC:2.5.1.9] [DE:RIBOFLAVIN SYNTHASE ALPHA CHAIN,] [SP:P50854] 179SPX2146 2146 4807 412 1236 1266 1.80E-170 [LN:GCH2_ACTPL] [AC:P50855][GN:RIBA] [OR:Actinobacillus pleuropneumoniae] [SR:,Haemophiluspleuropneumoniae] [EC:3.5.4.25] [DE:SYNTHASE)]] [SP:P50855] 153 SPX21472147 4808 156 468 546 1.30E-70 [LN:RISB_ACTPL] [AC:P50856] [GN:RIBH][OR:Actinobacillus pleuropneumoniae] [SR:,Haemophilus pleuropneumoniae][EC:2.5.1.9] [DE:(LUMAZINE SYNTHASE) (RIBOFLAVIN SYNTHASE BETA CHAIN)][SP:P50856] 194 SPX2148 2148 4809 650 1950 3286 0 [LN:HEXB_STRPN][AC:P14160] [GN:HEXB] [OR:Streptococcus pneumoniae] [DE:DNA MISMATCHREPAIR PROTEIN HEXB] [SP:P14160] 117 SPX2149 2149 4810 84 252 NO-HIT 6SPX2150 2150 4811 97 291 NO-HIT 6 SPX2151 2151 4812 61 183 122 1.10E-12[LN:T30285] [AC:T30285] [PN:hypothetical protein] [OR:Streptococcuspneumoniae] 79 SPX2152 2152 4813 174 522 231 9.30E-27 [GI:1196936][LN:STRHEXB] [AC:M29686] [PN:unknown protein] [OR:Streptococcuspneumoniae] [SR:Streptococcus pneumoniae (clone: pSP(8,41).) DNA] 144SPX2153 2153 4814 153 459 NO-HIT 6 SPX2154 2154 4815 126 378 3331.60E-40 [GI:517210] [LN:SPU11799] [AC:U11799] [OR:Streptococcuspyogenes] 65 SPX2155 2155 4816 211 633 762 7.90E-101 [GI:517210][LN:SPU11799] [AC:U11799] [OR:Streptococcus pyogenes] 65 SPX2156 21564817 201 603 499 7.70E-65 [LN:C81084] [AC:C81084] [PN:hypotheticalprotein NMB1426 [imported]] [GN:NMB1426] [OR:Neisseria meningitidis] 109SPX2157 2157 4818 64 192 NO-HIT 6 SPX2158 2158 4819 218 654 461 2.50E-67[LN:C81084] [AC:C81084] [PN:hypothetical protein NMB1426 [imported]][GN:NMB1426] [OR:Neisseria meningitidis] 109 SPX2159 2159 4820 201 603353 3.50E-53 [GI:6782392] [LN:SDY18363] [AC:Y18363] [PN:ribonucleotidereductase-like (Nrd-like)] [GN:nrd] [OR:Streptococcus dysgalactiae] 125SPX2160 2160 4821 194 582 NO-HIT 6 SPX2161 2161 4822 429 1287 21766.20E-298 [GI:5830536] [LN:SPAJ6396] [AC:AJ006396] [PN:responseregulator] [GN:rr07] [OR:Streptococcus pneumoniae] 104 SPX2162 2162 4823568 1704 1183 7.00E-160 [GI:5830535] [LN:SPAJ6396] [AC:AJ006396][PN:histidine kinase] [GN:hk07] [OR:Streptococcus pneumoniae] 102SPX2163 2163 4824 205 615 NO-HIT 6 SPX2164 2164 4825 190 570 NO-HIT 6SPX2165 2165 4826 231 693 395 1.90E-87 [GI:6165406] [LN:LLA012388][AC:AJ012388] [PN:hypothetical protein] [OR:Lactococcus lactis] 91SPX2166 2166 4827 354 1062 616 4.50E-130 [GI:6165405] [LN:LLA012388][AC:AJ012388] [PN:hypothetical protein] [OR:Lactococcus lactis] 91SPX2167 2167 4828 73 219 94 8.50E-07 [LN:G72536] [AC:G72536][PN:hypothetical protein APE1580] [GN:APE1580] [OR:Aeropyrum pernix] 92SPX2168 2168 4829 458 1374 219 7.10E-53 [LN:E75327] [AC:E75327][PN:ArgE/DapE/Acy1 family protein] [GN:DR2017] [OR:Deinococcusradiodurans] 99 SPX2169 2169 4830 285 855 319 1.50E-63 [GI:6165404][LN:LLA012388] [AC:AJ012388] [PN:hypothetical protein] [OR:Lactococcuslactis] 91 SPX2170 2170 4831 66 198 NO-HIT 6 SPX2171 2171 4832 184 552109 1.10E-12 [LN:YXEM_BACSU] [AC:P54952] [GN:YXEM:LP9E] [OR:Bacillussubtilis] [DE:INTERGENIC REGION PRECURSOR] [SP:P54952] 110 SPX2172 21724833 62 186 NO-HIT 6 SPX2173 2173 4834 225 675 129 5.60E-10 [LN:G75494][AC:G75494] [PN:AzlC family protein] [GN:DR0633] [CL:hypotheticalprotein b2682] [OR:Deinococcus radiodurans] 121 SPX2174 2174 4835 137411 328 2.80E-41 [LN:T30285] [AC:T30285] [PN:hypothetical protein][OR:Streptococcus pneumoniae] 79 SPX2175 2175 4836 80 240 NO-HIT 6SPX2176 2176 4837 75 225 NO-HIT 6 SPX2177 2177 4838 410 1230 80 2.70E-10[GI:3582221] [LN:AE001272] [AC:AE001272] [PN:conserved hypotheticalprotein] [GN:ORF00049] [OR:Lactococcus lactis] 114 SPX2178 2178 4839 222666 71 1.80E-05 [LN:E69787] [AC:E69787] [PN:hypothetical protein ydiL][GN:ydiL] [OR:Bacillus subtilis] 87 SPX2179 2179 4840 66 198 NO-HIT 6SPX2180 2180 4841 296 888 587 4.20E-77 [GI:4102023] [LN:AF007761][AC:AF007761] [PN:MutR] [GN:mutR] [FN:positive transcriptional regulatorof mutA] [OR:Streptococcus mutans] 134 SPX2181 2181 4842 69 207 NO-HIT 6SPX2182 2182 4843 206 618 479 1.40E-72 [LN:UDG5_ECOLI] [AC:Q47329][GN:KFID] [OR:Escherichia coli] [EC:1.1.1.22] [DE:(UDP-GLCDH) (UDPGDH)][SP:Q47329] 111 SPX2183 2183 4844 252 756 86 3.90E-08 [GI:4689219][LN:AF115779] [AC:AF115779] [PN:unknown] [GN:mitC] [OR:Streptomyceslavendulae] 92 SPX2184 2184 4845 74 222 NO-HIT 6 SPX2185 2185 4846 115345 NO-HIT 6 SPX2186 2186 4847 81 243 NO-HIT 6 SPX2187 2187 4848 5391617 294 1.70E-34 [LN:D72267] [AC:D72267] [PN:ABC transporter,ATP-binding protein] [GN:TM1328] [CL:unassigned ATP-binding cassetteproteins:ATP-binding cassette homology] [OR:Thermotoga maritima] 180SPX2188 2188 4849 318 954 137 5.90E-20 [LN:B75096] [AC:B75096][PN:glycosyl transferase PAB0772] [GN:PAB0772] [CL:Neisseriameningitidis glycosyl transferase A] [OR:Pyrococcus abyssi] 144 SPX21892189 4850 175 525 179 6.60E-17 [GI:1276880] [LN:STU40830] [AC:U40830][PN:EpsG] [GN:epsG] [OR:Streptococcus thermophilus] 90 SPX2190 2190 4851188 564 NO-HIT 6 SPX2191 2191 4852 107 321 187 3.70E-21 [GI:4200438][LN:AF026471] [AC:AF026471] [PN:putative transposase] [OR:Streptococcuspneumoniae] 96 SPX2192 2192 4853 88 264 196 2.60E-23 [GI:5019553][LN:SPN239004] [AC:AJ239004] [PN:putative transposase] [OR:Streptococcuspneumoniae] 97 SPX2193 2193 4854 355 1065 893 8.00E-121 [GI:2804700][LN:AF030361] [AC:AF030361] [PN:transposase] [OR:Streptococcuspneumoniae] 87 SPX2194 2194 4855 129 387 490 2.90E-65 [GI:663279][LN:STRCOMAA] [AC:M36180:L15190] [PN:transposase] [OR:Streptococcuspneumoniae] [SR:Streptococcus pneumoniae (strain RX1) DNA] 138 SPX21952195 4856 71 213 119 2.60E-10 [GI:2198546] [LN:SPCPS14E] [AC:X85787][GN:tasA] [OR:Streptococcus pneumoniae] 78 SPX2196 2196 4857 337 1011913 6.50E-132 [LN:YDIE_BACSU] [AC:O05518] [GN:YDIE] [OR:Bacillussubtilis] [DE:HYPOTHETICAL 36.8 KD PROTEIN IN PHOB-GROES INTERGENICREGION] [SP:O05518] 138 SPX2197 2197 4858 146 438 92 1.00E-09[LN:E69786] [AC:E69786] [PN:ribosomal-protein-alanine N-acetyltransferhomolog ydiD] [GN:ydiD] [CL:Escherichia coli ribosomal-protein-alanineN-acetyltransferase rimI] [OR:Bacillus subtilis] 190 SPX2198 2198 4859228 684 303 1.40E-53 [GI:3341437] [LN:EFY17797] [AC:Y17797][PN:hypothetical protein] [GN:ydiC] [OR:Enterococcus faecalis] 101SPX2199 2199 4860 62 186 NO-HIT 6 SPX2200 2200 4861 77 231 NO-HIT 6SPX2201 2201 4862 78 234 78 2.50E-10 [LN:D69871] [AC:D69871][PN:hypothetical protein ykzG] [GN:ykzG] [OR:Bacillus subtilis] 87SPX2202 2202 4863 560 1680 1841 6.00E-251 [LN:YKQC_BACSU] [AC:Q45493][GN:YKQC] [OR:Bacillus subtilis] [DE:HYPOTHETICAL 61.5 KD PROTEIN INADEC-PDHA INTERGENIC REGION] [SP:Q45493] 137 SPX2203 2203 4864 121 363NO-HIT 6 SPX2204 2204 4865 638 1914 1698 2.50E-282 [LN:GIDA_LACLC][AC:O32806] [GN:GIDA] [OR:Lactococcus lactis][SR:,subspcremoris:Streptococcus cremoris] [DE:GLUCOSE INHIBITEDDIVISION PROTEIN A (FRAGMENT)] [SP:O32806] 171 SPX2205 2205 4866 158 474NO-HIT 6 SPX2206 2206 4867 161 483 73 2.50E-06 [LN:F75354] [AC:F75354][PN:MutT/nudix family protein] [GN:DR1776] [OR:Deinococcus radiodurans]95 SPX2207 2207 4868 392 1176 578 1.10E-170 [LN:TRMU_BACSU] [AC:O35020][GN:TRMU] [OR:Bacillus subtilis] [EC:2.1.1.61] [DE:(EC 2.1.1.61)][SP:O35020] 105 SPX2208 2208 4869 60 180 NO-HIT 6 SPX2209 2209 4870 66198 NO-HIT 6 SPX2210 2210 4871 551 1653 1324 7.00E-210 [LN:A41971][AC:A41971:A60282:A33134] [PN:surface protein pspAprecursor:pneumococcal surface protein A] [GN:pspA] [CL:cpl repeathomology] [OR:Streptococcus pneumoniae] 169 SPX2211 2211 4872 79 237 981.60E-06 [GI:311109] [LN:YSCISCLRP] [AC:L16900] [PN:intrastrandcrosslink recognition protein] [GN:Ixr1] [OR:Saccharomyces cerevisiae][SR:Saccharomyces cerevisiae (strain ) DNA] 169 SPX2212 2212 4873 64 19277 0.00063 [LN:B72392] [AC:B72392] [PN:hypothetical protein] [GN:TM0315][OR:Thermotoga maritima] 86 SPX2213 2213 4874 103 309 87 0.0009[GI:7292943] [LN:AE003494] [AC:AE003494:AE002593] [GN:CG11075][OR:Drosophila melanogaster] [SR:fruit fly] 106 SPX2214 2214 4875 106318 NO-HIT 6 SPX2215 2215 4876 103 309 459 8.20E-56 [GI:6752385][LN:AF071807] [AC:AF071807] [PN:PspA] [GN:pspA] [OR:Streptococcuspneumoniae] 90 SPX2216 2216 4877 93 279 NO-HIT 6 SPX2217 2217 4878 100300 NO-HIT 6 SPX2218 2218 4879 71 213 NO-HIT 6 SPX2219 2219 4880 253 759NO-HIT 6 SPX2220 2220 4881 129 387 NO-HIT 6 SPX2221 2221 4882 301 903NO-HIT 6 SPX2222 2222 4883 61 183 NO-HIT 6 SPX2223 2223 4884 125 375NO-HIT 6 SPX2224 2224 4885 62 186 NO-HIT 6 SPX2225 2225 4886 227 681NO-HIT 6 SPX2226 2226 4887 76 228 NO-HIT 6 SPX2227 2227 4888 319 9571739 3.00E-234 [LN:ALYS_BPHB3] [AC:P32762] [GN:HBL] [OR:Streptococcuspneumoniae phage HB-3] [EC:3.5.1.28] [DE:LYTIC AMIDASE,(N-ACETYLMURAMOYL-L-ALANINE AMIDASE)] [SP:P32762] 162 SPX2228 2228 4889111 333 NO-HIT 6 SPX2229 2229 4890 139 417 97 1.20E-08 [LN:VG14_BPB03][AC:Q37895] [GN:14] [OR:Bacteriophage B103] [DE:LYSIS PROTEIN (LATEPROTEIN GP14)] [SP:Q37895] 110 SPX2230 2230 4891 117 351 NO-HIT 6SPX2231 2231 4892 68 204 NO-HIT 6 SPX2232 2232 4893 2120 6360 1541.40E-22 [GI:4530154] [LN:AF085222] [AC:AF085222] [PN:putative tail-hostspecificity protein] [OR:Streptococcus thermophilus bacteriophage DT1]134 SPX2233 2233 4894 79 237 NO-HIT 6 SPX2234 2234 4895 117 351 NO-HIT 6SPX2235 2235 4896 1218 3654 236 2.10E-30 [GI:2392838] [LN:AF011378][AC:AF011378] [PN:unknown] [OR:Bacteriophage sk1] 76 SPX2236 2236 4897187 561 106 2.00E-07 [GI:5305335] [LN:AF071081] [AC:AF071081][PN:proline-rich mucin homolog] [OR:Mycobacterium tuberculosis] 104SPX2237 2237 4898 70 210 NO-HIT 6 SPX2238 2238 4899 73 219 NO-HIT 6SPX2239 2239 4900 127 381 NO-HIT 6 SPX2240 2240 4901 138 414 NO-HIT 6SPX2241 2241 4902 123 369 77 0.00049 [LN:T13522] [AC:T13522][PN:hypothetical protein 33] [CL:Bacillus phage phi-105 hypotheticalprotein 33] [OR:Bacillus phage phi-105] 132 SPX2242 2242 4903 172 516 717.90E-06 [LN:T42287] [AC:T42287] [PN:hypothetical protein] [OR:phageSPP1] 65 SPX2243 2243 4904 61 183 NO-HIT 6 SPX2244 2244 4905 113 339NO-HIT 6 SPX2245 2245 4906 104 312 NO-HIT 6 SPX2246 2246 4907 63 189NO-HIT 6 SPX2247 2247 4908 61 183 73 0.0003 [LN:F75258] [AC:F75258][PN:hypothetical protein] [GN:DR2560] [OR:Deinococcus radiodurans] 90SPX2248 2248 4909 282 846 226 2.60E-48 [GI:1369939] [LN:BTP9011][AC:X84706] [PN:major head protein] [GN:mhp] [OR:Bacteriophage B1] 92SPX2249 2249 4910 195 585 NO-HIT 6 SPX2250 2250 4911 86 258 NO-HIT 6SPX2251 2251 4912 76 228 NO-HIT 6 SPX2252 2252 4913 468 1404 80 1.20E-06[LN:T13317] [AC:T13317] [PN:hypothetical protein 28] [OR:Streptococcusphage phi-O1205] 87 SPX2253 2253 4914 490 1470 154 3.40E-39 [LN:T13620][AC:T13620] [PN:hypothetical protein gp502] [OR:Streptococcus phagephi-Sfi11] 90 SPX2254 2254 4915 433 1299 330 6.80E-48 [LN:TERL_BPSPP][AC:P54308] [GN:2] [OR:Bacteriophage SPP1] [DE:TERMINASE LARGE SUBUNIT(G2P)] [SP:P54308] 105 SPX2255 2255 4916 160 480 215 2.30E-32[GI:4680607] [LN:AF125198] [AC:AF125198] [PN:terminase small subunit][GN:TS1] [OR:bacteriophage phi-FC1] 105 SPX2256 2256 4917 135 405 1544.60E-16 [GI:4530181] [LN:AF085222] [AC:AF085222] [PN:unknown][OR:Streptococcus thermophilus bacteriophage DT1] 103 SPX2257 2257 4918124 372 NO-HIT 6 SPX2258 2258 4919 146 438 115 1.00E-14 [GI:5001708][LN:AF109874] [AC:AF109874] [PN:unknown] [OR:Bacteriophage Tuc2009] 80SPX2259 2259 4920 153 459 NO-HIT 6 SPX2260 2260 4921 87 261 109 9.50E-12[GI:4530179] [LN:AF085222] [AC:AF085222] [PN:unknown] [OR:Streptococcusthermophilus bacteriophage DT1] 103 SPX2261 2261 4922 232 696 2031.70E-24 [LN:T13308] [AC:T13308] [PN:hypothetical protein 19][OR:Streptococcus phage phi-O1205] 87 SPX2262 2262 4923 450 1350 3581.30E-46 [GI:2689558] [LN:U93688] [AC:U93688] [OR:Staphylococcus aureus]63 SPX2263 2263 4924 274 822 470 7.10E-87 [LN:T13301] [AC:T13301][PN:hypothetical protein 12] [OR:Streptococcus phage phi-O1205] 87SPX2264 2264 4925 78 234 NO-HIT 6 SPX2265 2265 4926 66 198 NO-HIT 6SPX2266 2266 4927 169 507 NO-HIT 6 SPX2267 2267 4928 276 828 NO-HIT 6SPX2268 2268 4929 106 318 NO-HIT 6 SPX2269 2269 4930 398 1194 NO-HIT 6SPX2270 2270 4931 163 489 NO-HIT 6 SPX2271 2271 4932 120 360 NO-HIT 6SPX2272 2272 4933 161 483 256 2.10E-45 [GI:2352435] [LN:AF004379][AC:AF004379] [OR:Streptococcus thermophilus bacteriophage Sfi21] 92SPX2273 2273 4934 258 774 NO-HIT 6 SPX2274 2274 4935 77 231 NO-HIT 6SPX2275 2275 4936 114 342 NO-HIT 6 SPX2276 2276 4937 63 189 NO-HIT 6SPX2277 2277 4938 87 261 NO-HIT 6 SPX2278 2278 4939 91 273 NO-HIT 6SPX2279 2279 4940 80 240 NO-HIT 6 SPX2280 2280 4941 64 192 NO-HIT 6SPX2281 2281 4942 68 204 NO-HIT 6 SPX2282 2282 4943 67 201 NO-HIT 6SPX2283 2283 4944 72 216 101 3.70E-09 [LN:Y272_METJA] [AC:Q57720][GN:MJ0272] [OR:Methanococcus jannaschii] [DE:HYPOTHETICALTRANSCRIPTIONAL REGULATOR MJ0272] [SP:Q57720] 132 SPX2284 2284 4945 68204 NO-HIT 6 SPX2285 2285 4946 230 690 NO-HIT 6 SPX2286 2286 4947 264792 112 4.00E-15 [LN:T13264] [AC:T13264] [PN:repressor protein][OR:Lactococcus lactis phage BK5-T] 82 SPX2287 2287 4948 317 951 1025.00E-09 [LN:F59095] [AC:F59095] [PN:hypothetical protein pXO1-38][GN:pXO1-38] [OR:Bacillus anthracis] 94 SPX2288 2288 4949 58 174 NO-HIT6 SPX2289 2289 4950 376 1128 212 3.50E-43 [GI:2689564] [LN:U93688][AC:U93688] [PN:integrase] [GN:int] [OR:Staphylococcus aureus] 87SPX2290 2290 4951 62 186 NO-HIT 6 SPX2291 2291 4952 353 1059 81 0.00071[LN:AF147045] [AC:AF147045] [PN:cytochrome c oxidase subunit 1] [GN:COI][OR:Mitochondrion Dolichoderus lutosus] [SR:Dolichoderus lutosus] 138SPX2292 2292 4953 64 192 NO-HIT 6 SPX2293 2293 4954 71 213 NO-HIT 6SPX2294 2294 4955 81 243 NO-HIT 6 SPX2295 2295 4956 149 447 NO-HIT 6SPX2296 2296 4957 60 180 NO-HIT 6 SPX2297 2297 4958 117 351 137 3.30E-14[GI:4760910] [LN:AF099088] [AC:AF099088] [PN:EntT] [GN:entT][OR:Enterococcus faecium] 86 SPX2298 2298 4959 288 864 117 4.70E-08[GI:4102023] [LN:AF007761] [AC:AF007761] [PN:MutR] [GN:mutR][FN:positive transcriptional regulator of mutA] [OR:Streptococcusmutans] 134 SPX2299 2299 4960 125 375 NO-HIT 6 SPX2300 2300 4961 76 228NO-HIT 6 SPX2301 2301 4962 127 381 NO-HIT 6 SPX2302 2302 4963 75 225NO-HIT 6 SPX2303 2303 4964 70 210 NO-HIT 6 SPX2304 2304 4965 68 204NO-HIT 6 SPX2305 2305 4966 288 864 117 4.70E-08 [GI:4102023][LN:AF007761] [AC:AF007761] [PN:MutR] [GN:mutR] [FN:positivetranscriptional regulator of mutA] [OR:Streptococcus mutans] 134 SPX23062306 4967 173 519 840 6.50E-114 [GI:663278] [LN:STRCOMAA][AC:M36180:L15190] [PN:transposase] [OR:Streptococcus pneumoniae][SR:Streptococcus pneumoniae (strain RX1) DNA] 138 SPX2307 2307 4968 122366 NO-HIT 6 SPX2308 2308 4969 96 288 279 1.60E-35 [GI:663279][LN:STRCOMAA] [AC:M36180:L15190] [PN:transposase] [OR:Streptococcuspneumoniae] [SR:Streptococcus pneumoniae (strain RX1) DNA] 138 SPX23092309 4970 256 768 1235 1.10E-172 [GI:663279] [LN:STRCOMAA][AC:M36180:L15190] [PN:transposase] [OR:Streptococcus pneumoniae][SR:Streptococcus pneumoniae (strain RX1) DNA] 138 SPX2310 2310 4971 157471 375 6.90E-56 [LN:ASSY_BACSU] [AC:O34347] [GN:ARGG] [OR:Bacillussubtilis] [EC:6.3.4.5] [DE:LIGASE)] [SP:O34347] 98 SPX2311 2311 4972 266798 200 6.10E-32 [LN:B72357] [AC:B72357] [PN:amino acid ABC transporter,periplasmic amino acid-binding protein] [GN:TM0593][CL:lysine-arginine-ornithine-binding protein] [OR:Thermotoga maritima]181 SPX2312 2312 4973 214 642 420 1.80E-51 [LN:F81408] [AC:F81408][PN:ABC-type transmembrane transport protein Cj0607 [imported]][GN:Cj0607] [OR:Campylobacter jejuni] 125 SPX2313 2313 4974 59 177 801.80E-07 [LN:F72598] [AC:F72598] [PN:hypothetical protein APE1254][GN:APE1254] [OR:Aeropyrum pernix] 92 SPX2314 2314 4975 439 1317 NO-HIT6 SPX2315 2315 4976 371 1113 NO-HIT 6 SPX2316 2316 4977 72 216 NO-HIT 6SPX2317 2317 4978 84 252 NO-HIT 6 SPX2318 2318 4979 288 864 117 4.70E-08[GI:4102023] [LN:AF007761] [AC:AF007761] [PN:MutR] [GN:mutR][FN:positive transcriptional regulator of mutA] [OR:Streptococcusmutans] 134 SPX2319 2319 4980 196 588 300 1.00E-34 [GI:1619598][LN:LGAPFA] [AC:Y08498] [PN:aggregation promoting protein] [GN:apfA][OR:Lactobacillus gasseri] 108 SPX2320 2320 4981 97 291 NO-HIT 6 SPX23212321 4982 224 672 276 8.70E-69 [LN:SDHB_BACSU] [AC:O34635] [GN:YLOW][OR:Bacillus subtilis] [EC:4.2.1.13] [DE:DEAMINASE) (SDH) (L-SD)][SP:O34635] 115 SPX2322 2322 4983 291 873 877 9.00E-119 [LN:SDHA_BACSU][AC:O34607] [GN:YLPA] [OR:Bacillus subtilis] [EC:4.2.1.13][DE:DEAMINASE) (SDH) (L-SD)] [SP:O34607] 115 SPX2323 2323 4984 178 534NO-HIT 6 SPX2324 2324 4985 211 633 123 1.50E-15 [GI:7576264][LN:ECH277403] [AC:AJ277403] [PN:IndB protein] [GN:indB] [OR:Erwiniachrysanthemi] 95 SPX2325 2325 4986 72 216 NO-HIT 6 SPX2326 2326 4987 6171851 1006 3.00E-136 [GI:6601348] [LN:AF155805] [AC:AF155805] [PN:Cps9E][GN:cps9E] [OR:Streptococcus suis] 86 SPX2327 2327 4988 84 252 1356.70E-14 [LN:S28486] [AC:S28486] [PN:hypothetical protein 2] [OR:Vibriocholerae] 72 SPX2328 2328 4989 392 1176 123 7.20E-25 [LN:T44514][AC:T44514] [PN:hypothetical protein 6P [imported]] [OR:Plesiomonasshigelloides] 93 SPX2329 2329 4990 102 306 NO-HIT 6 SPX2330 2330 4991249 747 142 5.40E-29 [LN:YYCB_BACSU] [AC:P37482] [GN:YYCB] [OR:Bacillussubtilis] [DE:HYPOTHETICAL 43.2 KD PROTEIN IN DNAC-RPLI INTERGENICREGION] [SP:P37482] 137 SPX2331 2331 4992 143 429 143 9.10E-15[LN:PQ0016] [AC:PQ0016] [PN:hypothetical 9K protein] [OR:Lactobacillusconfusus] 80 SPX2332 2332 4993 109 327 102 4.10E-07 [LN:D75250][AC:D75250] [PN:conserved hypothetical protein] [GN:DR2629][OR:Deinococcus radiodurans] 100 SPX2333 2333 4994 198 594 NO-HIT 6SPX2334 2334 4995 304 912 NO-HIT 6 SPX2335 2335 4996 123 369 NO-HIT 6SPX2336 2336 4997 355 1065 118 3.00E-07 [LN:T18283] [AC:T18283][PN:hypothetical protein G5] [OR:Dictyostelium discoideum] 82 SPX23372337 4998 318 954 NO-HIT 6 SPX2338 2338 4999 329 987 925 1.60E-165[GI:2565150] [LN:LLU92974] [AC:U92974:M90760:M90761] [PN:unknown][OR:Lactococcus lactis] 89 SPX2339 2339 5000 69 207 NO-HIT 6 SPX23402340 5001 515 1545 NO-HIT 6 SPX2341 2341 5002 134 402 NO-HIT 6 SPX23422342 5003 308 924 389 1.50E-61 [GI:1483212] [LN:ATCELD] [AC:Z77855][PN:sugar-binding transport protein] [OR:Anaerocellum thermophilum] 104SPX2343 2343 5004 320 960 601 9.60E-95 [GI:1483211] [LN:ATCELD][AC:Z77855] [PN:sugar-binding transport protein] [OR:Anaerocellumthermophilum] 104 SPX2344 2344 5005 70 210 NO-HIT 6 SPX2345 2345 5006120 360 NO-HIT 6 SPX2346 2346 5007 116 348 577 5.80E-76 [GI:4200438][LN:AF026471] [AC:AF026471] [PN:putative transposase] [OR:Streptococcuspneumoniae] 96 SPX2347 2347 5008 177 531 299 3.70E-73 [LN:A37146][AC:A37146:A44901:S11354:C69699:I39962] [PN:ribosomal proteinS4:ribosomal protein BS4 (rpsD)] [GN:rpsD] [CL:Escherichia coliribosomal protein S4] [OR:Bacillus subtilis] 182 SPX2348 2348 5009 3591077 1709 2.00E-231 [GI:5830539] [LN:SPAJ6397] [AC:AJ006397][PN:histidine kinase] [GN:hk08] [OR:Streptococcus pneumoniae] 102SPX2349 2349 5010 233 699 1196 1.40E-161 [GI:5830538] [LN:SPAJ6397][AC:AJ006397] [PN:response regulator] [GN:rr08] [OR:Streptococcuspneumoniae] 104 SPX2350 2350 5011 124 372 NO-HIT 6 SPX2351 2351 5012 8912673 106 0.00022 [GI:7293562] [LN:AE003511] [AC:AE003511:AE002593][GN:CG7874] [OR:Drosophila melanogaster] [SR:fruit fly] 105 SPX2352 23525013 190 570 NO-HIT 6 SPX2353 2353 5014 137 411 NO-HIT 6 SPX2354 23545015 179 537 199 2.70E-20 [GI:3550634] [LN:SPAJ6986] [AC:AJ006986][PN:glycosyl transferase] [GN:cap33fH] [FN:synthesis of capsularpolysaccharide] [OR:Streptococcus pneumoniae] 151 SPX2355 2355 5016 222666 346 1.00E-42 [LN:YKQB_BACSU] [AC:P39760] [GN:YKQB] [OR:Bacillussubtilis] [DE:HYPOTHETICAL 24.3 KD PROTEIN IN KINC-ADEC INTERGENICREGION (ORF4)] [SP:P39760] 144 SPX2356 2356 5017 460 1380 339 7.90E-94[LN:G75367] [AC:G75367] [PN:potassium uptake protein KtrB] [GN:DR1668][OR:Deinococcus radiodurans] 99 SPX2357 2357 5018 62 186 162 1.60E-17[LN:T30285] [AC:T30285] [PN:hypothetical protein] [OR:Streptococcuspneumoniae] 79 SPX2358 2358 5019 255 765 75 8.50E-08 [LN:D72516][AC:D72516] [PN:probable uridine phosphorylase APE2105] [GN:APE2105][CL:purine-nucleoside phosphorylase pnp] [OR:Aeropyrum pernix] 143SPX2359 2359 5020 63 189 91 8.80E-06 [GI:6332762] [LN:AB033763][AC:AB033763:AB014419:AB014429:AB014439] [PN:hypothetical protein][OR:Staphylococcus aureus] [SR:Staphylococcus aureus (strain:NCTC10442)DNA, clone_lib:Lambda das] 194 SPX2360 2360 5021 99 297 153 6.00E-20[LN:YQHL_BACSU] [AC:P54510] [GN:YQHL] [OR:Bacillus subtilis][DE:HYPOTHETICAL 14.6 KD PROTEIN IN GCVT-SPOIIIAA INTERGENIC REGION][SP:P54510] 141 SPX2361 2361 5022 121 363 NO-HIT 6 SPX2362 2362 5023 98294 194 1.30E-21 [GI:6332750] [LN:AB033763][AC:AB033763:AB014419:AB014429:AB014439] [PN:hypothetical protein][OR:Staphylococcus aureus] [SR:Staphylococcus aureus (strain:NCTC10442)DNA, clone_lib:Lambda das] 194 SPX2363 2363 5024 82 246 167 8.40E-17[LN:A75356] [AC:A75356] [PN:conserved hypothetical protein] [GN:DR1764][OR:Deinococcus radiodurans] 100 SPX2364 2364 5025 132 396 175 2.80E-26[LN:T44495] [AC:T44495] [PN:hypothetical protein YFIE [imported]][OR:Bacillus halodurans] 90 SPX2365 2365 5026 346 1038 219 2.60E-44[GI:6562808] [LN:SC4A7] [AC:AL133423] [PN:putative aldose 1-epimerase][GN:SC4A7.35] [OR:Streptomyces coelicolor A3(2)] 119 SPX2366 2366 5027153 459 NO-HIT 6 SPX2367 2367 5028 389 1167 473 3.90E-95 [LN:AGAS_ECOLI][AC:P42907] [GN:AGAS] [OR:Escherichia coli] [DE:AGAS PROTEIN][SP:P42907] 89 SPX2368 2368 5029 83 249 77 6.20E-05 [GI:1914870][LN:SPZ82001] [AC:Z82001] [PN:unknown] [OR:Streptococcus pneumoniae] 81SPX2369 2369 5030 135 405 103 3.80E-13 [GI:5669855] [LN:AF130465][AC:AF130465] [PN:mannose-specific phosphotransferase system] [GN:manL][OR:Streptococcus salivarius] 128 SPX2370 2370 5031 277 831 144 4.90E-34[LN:PTPD_ECOLI] [AC:P42911] [GN:AGAD] [OR:Escherichia coli] [DE:ENZYMEII, D COMPONENT)] [SP:P42911] 102 SPX2371 2371 5032 302 906 128 6.60E-16[GI:1732200] [LN:VFU65015] [AC:U65015] [PN:PTS permease for mannosesubunit IIPMan] [GN:manY] [OR:Vibrio furnissii] 115 SPX2372 2372 5033159 477 298 2.50E-36 [GI:6690421] [LN:AF129168] [AC:AF129168] [PN:EIIBsorbose-PTS homolog] [GN:sorB] [OR:Lactobacillus casei] 105 SPX2373 23735034 509 1527 265 3.30E-90 [LN:JC5618] [AC:JC5618][PN:beta-galactosidase,:lactase] [GN:bgaC] [CL:beta-galactosidase bga][OR:Bacillus circulans] [EC:3.2.1.23] 134 SPX2374 2374 5035 131 393 3585.70E-44 [LN:JC5618] [AC:JC5618] [PN:beta-galactosidase,:lactase][GN:bgaC] [CL:beta-galactosidase bga] [OR:Bacillus circulans][EC:3.2.1.23] 134 SPX2375 2375 5036 239 717 142 7.80E-15 [LN:F69750][AC:F69750] [PN:transcription regulator GntR family homolog ybgA][GN:ybgA] [CL:transcription regulator GntR] [OR:Bacillus subtilis] 144SPX2376 2376 5037 1304 3912 6324 0 [LN:STRH_STRPN] [AC:P49610] [GN:STRH][OR:Streptococcus pneumoniae] [EC:3.2.1.52][DE:BETA-N-ACETYLHEXOSAMINIDASE PRECURSOR,] [SP:P49610] 139 SPX2377 23775038 130 390 NO-HIT 6 SPX2378 2378 5039 433 1299 1678 1.40E-227[LN:PUR8_BACSU] [AC:P12047] [GN:PURB:PURE] [OR:Bacillus subtilis][EC:4.3.2.2] [DE:(GLUTAMYL-TRNA SYNTHETASE REGULATORY FACTOR)][SP:P12047] 140 SPX2379 2379 5040 76 228 NO-HIT 6 SPX2380 2380 5041 3841152 286 1.70E-65 [GI:5051462] [LN:NME242842] [AC:AJ242842] [PN:putativephosphoribosylaminoimidazole] [GN:purK] [FN:purine nucleotide synthesis][OR:Neisseria meningitidis] 155 SPX2381 2381 5042 155 465 515 5.30E-66[GI:3892884] [LN:LLJ000883] [AC:AJ000883] [GN:purE] [OR:Lactococcuslactis] 75 SPX2382 2382 5043 421 1263 589 2.10E-157 [GI:3892883][LN:LLJ000883] [AC:AJ000883] [GN:purD] [OR:Lactococcus lactis] 75SPX2383 2383 5044 227 681 NO-HIT 6 SPX2384 2384 5045 523 1569 8812.30E-213 [LN:PUR9_BACSU] [AC:P12048] [GN:PURH:PURHJ] [OR:Bacillussubtilis] [EC:2.1.2.3:3.5.4.10] [DE:(IMP SYNTHETASE) (ATIC)]][SP:P12048] 130 SPX2385 2385 5046 170 510 136 9.10E-15 [LN:VANZ_ENTFC][AC:Q06242] [GN:VANZ] [OR:Enterococcus faecium] [SR:,Streptococcusfaecium] [DE:VANZ PROTEIN] [SP:Q06242] 123 SPX2386 2386 5047 116 348NO-HIT 6 SPX2387 2387 5048 182 546 553 2.20E-72 [GI:6446399][LN:SPU70775] [AC:U70775] [PN:phosphoribosylglycinamideformyltransferase] [OR:Streptococcus pyogenes] 115 SPX2388 2388 5049 3411023 1084 7.20E-148 [GI:3150047] [LN:AF016634] [AC:AF016634][PN:phosphoribosylformylglycinamide cyclo-ligase] [GN:pur5][OR:Lactococcus lactis subsp. cremoris] 140 SPX2389 2389 5050 481 14431727 7.50E-248 [GI:4097534] [LN:LLU64311] [AC:U64311][PN:phosphoribosylpyrophosphate amidotransferase] [GN:purF][OR:Lactococcus lactis] 122 SPX2390 2390 5051 1243 3729 149 3.00E-49[LN:C69492] [AC:C69492] [PN:phosphoribosylformylglycinamidine synthase,component II:formylglycinamide ribotideamidotransferase:phosphoribosylformylglycinamidine synthetase][OR:Archaeoglobus fulgidus] [EC:6.3.5.3] 217 SPX2391 2391 5052 45 135NO-HIT 6 SPX2392 2392 5053 204 612 875 9.90E-117 [LN:PUR7_STRPN][AC:Q07296] [GN:PURC] [OR:Streptococcus pneumoniae] [EC:6.3.2.6][DE:(SAICAR SYNTHETASE)] [SP:Q07296] 117 SPX2393 2393 5054 124 372 1751.90E-17 [LN:H75412] [AC:H75412] [PN:spermidine/putrescine ABCtransporter, periplasmic spermidine/putrescine-binding protein][GN:DR1305] [OR:Deinococcus radiodurans] 160 SPX2394 2394 5055 431 12932159 2.90E-302 [GI:2804700] [LN:AF030361] [AC:AF030361] [PN:transposase][OR:Streptococcus pneumoniae] 87 SPX2395 2395 5056 86 258 NO-HIT 6SPX2396 2396 5057 166 498 300 8.70E-37 [LN:YEBR_ECOLI][AC:P76270:O07976:O07978] [GN:YEBR] [OR:Escherichia coli][DE:HYPOTHETICAL 20.3 KD PROTEIN IN PRC-PPHA INTERGENIC REGION][SP:P76270:O07976:O07978] 163 SPX2397 2397 5058 552 1656 749 7.10E-135[LN:S13786] [AC:S13786:S00745:S66049:B69618] [PN:DNA-directed DNApolymerase, III chain dnaX:DNA polymerase III (gamma and tau subunits)dnaX] [GN:dnaX:dnaZX] [CL:DNA-directed DNA polymerase III gamma chain][OR:Bacillus subtilis] [EC:2.7.7.7] 245 SPX2398 2398 5059 65 195 NO-HIT6 SPX2399 2399 5060 257 771 948 1.70E-125 [LN:V296_BACSU] [AC:P80866][GN:YURI] [OR:Bacillus subtilis] [DE:VEGETATIVE PROTEIN 296 (VEG296)][SP:P80866] 109 SPX2400 2400 5061 420 1260 583 1.90E-87 [LN:G70019][AC:G70019] [PN:conserved hypothetical protein yurX] [GN:yurX][CL:Methanobacterium thermoautotrophicum ABC transporter Ycf24][OR:Bacillus subtilis] 161 SPX2401 2401 5062 409 1227 622 8.60E-181[LN:F70019] [AC:F70019] [PN:nifS protein homolog yurW] [GN:yurW][CL:nifS protein] [OR:Bacillus subtilis] 105 SPX2402 2402 5063 157 471229 1.90E-43 [LN:E70019] [AC:E70019] [PN:nitrogen fixation protein nifUhomolog yurV] [GN:yurV] [CL:Yeast nitrogen fixation protein:nitrogenfixation protein homology] [OR:Bacillus subtilis] 177 SPX2403 2403 5064470 1410 1721 1.20E-229 [LN:D70019] [AC:D70019] [PN:conservedhypothetical protein yurU] [GN:yurU] [CL:Methanobacteriumthermoautotrophicum ABC transporter Ycf24] [OR:Bacillus subtilis] 161SPX2404 2404 5065 65 195 NO-HIT 6 SPX2405 2405 5066 62 186 112 8.10E-11[LN:T30285] [AC:T30285] [PN:hypothetical protein] [OR:Streptococcuspneumoniae] 79 SPX2406 2406 5067 414 1242 2059 6.00E-276 [GI:1620468][LN:SPDACAO] [AC:X99400] [PN:D,D-carboxypeptidase] [GN:dacA][OR:Streptococcus pneumoniae] 105 SPX2407 2407 5068 370 1110 18075.00E-255 [GI:1620467] [LN:SPDACAO] [AC:X99400] [PN:membrane protein][OR:Streptococcus pneumoniae] 89 SPX2408 2408 5069 73 219 NO-HIT 6SPX2409 2409 5070 67 201 NO-HIT 6 SPX2410 2410 5071 247 741 258 7.40E-41[LN:B69627] [AC:B69627] [PN:transcription repressor of fructose operonfruR] [GN:fruR] [CL:regulatory protein gutR] [OR:Bacillus subtilis] 138SPX2411 2411 5072 304 912 725 2.80E-94 [LN:A69627] [AC:A69627][PN:fructose 1-phosphate kinase fruB] [GN:fruB][CL:6-phosphofructokinase 2] [OR:Bacillus subtilis] 123 SPX2412 24125073 76 228 NO-HIT 6 SPX2413 2413 5074 651 1953 371 4.60E-168[LN:H69626] [AC:H69626] [PN:PTS fructose-specific enzyme IIBC componentfruA] [GN:fruA] [CL:phosphotransferase system enzyme II,fructose-specific:phosphotransferase system mannitol-specific enzyme IIfactor III homology] [OR:Bacillus subtilis] 246 SPX2414 2414 5075 7382214 934 4.10E-198 [LN:SP3E_BACSU] [AC:P21458:P21459] [GN:SPOIIIE][OR:Bacillus subtilis] [DE:STAGE III SPORULATION PROTEIN E][SP:P21458:P21459] 126 SPX2415 2415 5076 84 252 82 0.00017 [GI:2257458][LN:AB000222] [AC:AB000222] [GN:epr] [FN:glycylglycine endopeptidaseresistance] [OR:Staphylococcus capitis] [SR:Staphylococcus capitis DNA]153 SPX2416 2416 5077 95 285 124 7.00E-12 [LN:A70132] [AC:A70132][PN:cell division protein homolog] [OR:Borrelia burgdorferi] [SR:, Lymedisease spirochete] 117 SPX2417 2417 5078 72 216 NO-HIT 6 SPX2418 24185079 220 660 102 0.00013 [LN:T06029] [AC:T06029] [PN:hypotheticalprotein T28I19.100] [GN:T28I19.100] [OR:Arabidopsis thaliana] [SR:,mouse-ear cress] 127 SPX2419 2419 5080 401 1203 698 8.70E-120[LN:NIFS_LACDE] [AC:P31672] [OR:Lactobacillus delbrueckii][SR:,subspbulgaricus] [DE:NIFS PROTEIN HOMOLOG (FRAGMENT)] [SP:P31672]131 SPX2420 2420 5081 405 1215 982 1.40E-130 [LN:THII_BACSU] [AC:O34595][GN:THII] [OR:Bacillus subtilis] [DE:PROBABLE THIAMINE BIOSYNTHESISPROTEIN THII] [SP:O34595] 121 SPX2421 2421 5082 210 630 115 3.40E-15[LN:G75475] [AC:G75475] [PN:conserved hypothetical protein] [GN:DR0779][OR:Deinococcus radiodurans] 100 SPX2422 2422 5083 116 348 NO-HIT 6SPX2423 2423 5084 112 336 NO-HIT 6 SPX2424 2424 5085 144 432 NO-HIT 6SPX2425 2425 5086 61 183 NO-HIT 6 SPX2426 2426 5087 389 1167 82 2.50E-06[LN:T35924] [AC:T35924] [PN:hypothetical protein SC9B5.04] [GN:SC9B5.04][OR:Streptomyces coelicolor] 101 SPX2427 2427 5088 498 1494 137 2.50E-32[GI:1841495] [LN:SEHSDRMS] [AC:Y11005] [PN:StySKI methylase] [GN:hsdM][OR:Salmonella enterica] 95 SPX2428 2428 5089 374 1122 109 3.30E-14[LN:YC18_METJA] [AC:Q58615] [GN:MJ1218] [OR:Methanococcus jannaschii][DE:HYPOTHETICAL PROTEIN MJ1218] [SP:Q58615] 114 SPX2429 2429 5090 79237 NO-HIT 6 SPX2430 2430 5091 138 414 NO-HIT 6 SPX2431 2431 5092 276828 153 1.90E-22 [LN:A75153] [AC:A75153] [PN:integrase/recombinase xerdPAB0255] [GN:xerD-like:PAB0255] [CL:probable site-specificintegrase/recombinase XerC] [OR:Pyrococcus abyssi] 164 SPX2432 2432 5093369 1107 148 4.50E-19 [GI:3057063] [LN:AF013165] [AC:AF013165] [PN:HsdS][GN:hsds] [OR:Lactococcus lactis] 84 SPX2433 2433 5094 1117 3351 1536.50E-30 [LN:T1R_ECOLI] [AC:P08956] [GN:HSDR:HSR] [OR:Escherichia coli][EC:3.1.21.3] [DE:TYPE I RESTRICTION ENZYME ECOK I R PROTEIN,][SP:P08956] 139 SPX2434 2434 5095 157 471 132 1.60E-24 [LN:AHRC_BACSU][AC:P17893] [GN:AHRC] [OR:Bacillus subtilis] [DE:ARGININE HYDROXIMATERESISTANCE PROTEIN] [SP:P17893] 117 SPX2435 2435 5096 758 2274 12981.20E-249 [LN:PEPX_LACLC] [AC:P22093] [GN:PEPX] [OR:Lactococcus lactis][SR:,subspcremoris:Streptococcus cremoris] [EC:3.4.14.11] [DE:PEPTIDASE)(X-PROLYL-DIPEPTIDYL AMINOPEPTIDASE) (X-PDAP)] [SP:P22093] 195 SPX24362436 5097 1034 3102 563 5.40E-170 [LN:DP3A_BACSU] [AC:O34623] [GN:DNAE][OR:Bacillus subtilis] [EC:2.7.7.7] [DE:DNA POLYMERASE III, ALPHACHAIN,] [SP:O34623] 125 SPX2437 2437 5098 63 189 NO-HIT 6 SPX2438 24385099 336 1008 1356 2.50E-182 [LN:K6PF_LACLA] [AC:Q07636] [GN:PFKA:PFK][OR:Lactococcus lactis] [SR:,subsplactis:Streptococcus lactis][EC:2.7.1.11] [DE:(PHOSPHOHEXOKINASE)] [SP:Q07636] 157 SPX2439 2439 5100236 708 1007 8.20E-134 [GI:6708108] [LN:AF172173] [AC:AF172173][PN:pyruvate kinase] [GN:pyk] [FN:conversion of phosphoenolpyruvate topyruvate] [OR:Streptococcus thermophilus] 153 SPX2440 2440 5101 305 9151099 9.10E-150 [GI:6708108] [LN:AF172173] [AC:AF172173] [PN:pyruvatekinase] [GN:pyk] [FN:conversion of phosphoenolpyruvate to pyruvate][OR:Streptococcus thermophilus] 153 SPX2441 2441 5102 74 222 1371.60E-13 [LN:G71171] [AC:G71171] [PN:hypothetical protein PH0571][GN:PH0571] [OR:Pyrococcus horikoshii] 95 SPX2442 2442 5103 67 201 733.00E-08 [LN:VINT_BPL54] [AC:P20709] [GN:INT] [OR:Bacteriophage L54a][DE:INTEGRASE] [SP:P20709] 87 SPX2443 2443 5104 101 303 95 3.10E-05[GI:763050] [LN:BTU21935] [AC:U21935] [PN:repressor protein][OR:Bacteriophage T270] 84 SPX2444 2444 5105 85 255 89 1.90E-08[GI:509672] [LN:TU2CIRPRSR] [AC:L26219] [PN:repressor protein] [GN:cI][OR:Bacteriophage Tuc2009] [SR:Bacteriophage Tuc2009 DNA] 128 SPX24452445 5106 291 873 393 1.90E-60 [GI:4580015] [LN:AF049342] [AC:AF049342][PN:unknown] [OR:Treponema denticola] 78 SPX2446 2446 5107 128 384 3643.60E-46 [LN:S52544] [AC:S52544] [PN:ISL2 protein] [OR:Lactobacillushelveticus] 71 SPX2447 2447 5108 104 312 NO-HIT 6 SPX2448 2448 5109 239717 NO-HIT 6 SPX2449 2449 5110 132 396 NO-HIT 6 SPX2450 2450 5111 272816 184 2.20E-58 [LN:D69759] [AC:D69759] [PN:hypothetical protein ycgQ][GN:ycgQ] [CL:Bacillus subtilis hypothetical protein ycgQ] [OR:Bacillussubtilis] 136 SPX2451 2451 5112 302 906 369 7.00E-86 [LN:E69759][AC:E69759] [PN:hypothetical protein ycgR] [GN:ycgR] [OR:Bacillussubtilis] 87 SPX2452 2452 5113 710 2130 644 1.20E-222 [LN:G69773][AC:G69773] [PN:conserved hypothetical protein ydcI] [GN:ydcI][CL:hypothetical protein ydcI] [OR:Bacillus subtilis] 128 SPX2453 24535114 150 450 256 7.80E-44 [GI:7007441] [LN:AB031213] [AC:AB031213][PN:YdcK] [GN:ydcK] [OR:Bacillus halodurans] [SR:Bacillus halodurans(strain:C-125) DNA] 129 SPX2454 2454 5115 85 255 90 7.80E-11 [LN:E70043][AC:E70043] [PN:hypothetical protein yvlC] [GN:yvlC] [OR:Bacillussubtilis] 87 SPX2455 2455 5116 64 192 NO-HIT 6 SPX2456 2456 5117 253 759486 8.70E-81 [LN:A70001] [AC:A70001] [PN:ABC transporter (ATP-bindingprotein) homolog ytsC] [GN:ytsC] [CL:unassigned ATP-binding cassetteproteins:ATP-binding cassette homology] [OR:Bacillus subtilis] 188SPX2457 2457 5118 75 225 76 3.20E-05 [LN:G72510] [AC:G72510][PN:hypothetical protein APE2061] [GN:APE2061] [OR:Aeropyrum pernix] 92SPX2458 2458 5119 663 1989 249 1.70E-50 [LN:B70001] [AC:B70001] [PN:ABCtransporter (permease) homolog ytsD] [GN:ytsD] [OR:Bacillus subtilis]101 SPX2459 2459 5120 197 591 230 2.10E-25 [LN:SPBC1683] [AC:AL355920][PN:hypothetical protein] [GN:SPBC1683.10c] [OR:Schizosaccharomycespombe] [SR:fission yeast] 121 SPX2460 2460 5121 365 1095 1143 8.40E-154[GI:517210] [LN:SPU11799] [AC:U11799] [OR:Streptococcus pyogenes] 65SPX2461 2461 5122 61 183 NO-HIT 6 SPX2462 2462 5123 492 1476 5853.60E-138 [LN:DCLY_BACSU] [AC:P21885:P26934] [GN:CAD] [OR:Bacillussubtilis] [EC:4.1.1.18] [DE:LYSINE DECARBOXYLASE, (LDC)][SP:P21885:P26934] 134 SPX2463 2463 5124 79 237 NO-HIT 6 SPX2464 24645125 176 528 83 1.20E-07 [GI:6009430] [LN:AB024946] [AC:AB024946][GN:orf54] [OR:Escherichia coli] [SR:Escherichia coli(sub_species:enteropathogenic, strain:B171] 140 SPX2465 2465 5126 287861 439 5.40E-79 [LN:SPEE_BACSU] [AC:P70998] [GN:SPEE] [OR:Bacillussubtilis] [EC:2.5.1.16] [DE:(SPDSY)] [SP:P70998] 99 SPX2466 2466 5127420 1260 1090 2.30E-187 [LN:C81435] [AC:C81435] [PN:hypothetical proteinCj0172c [imported]] [GN:Cj0172c] [OR:Campylobacter jejuni] 107 SPX24672467 5128 376 1128 411 7.60E-103 [LN:E75398] [AC:E75398][PN:carboxynorspermidine decarboxylase] [GN:DR1410] [OR:Deinococcusradiodurans] 104 SPX2468 2468 5129 362 1086 530 3.80E-94 [GI:5712716][LN:AF153708] [AC:AF153708] [PN:unknown] [OR:Pseudomonas sp. BG33R] 80SPX2469 2469 5130 292 876 585 1.20E-110 [GI:5262946] [LN:LES19104][AC:Y19104] [PN:beta-alanine synthase] [OR:Lycopersicon esculentum][SR:tomato] 106 SPX2470 2470 5131 270 810 209 6.80E-43 [LN:YXEH_BACSU][AC:P54947] [GN:YXEH:IP1B] [OR:Bacillus subtilis] [DE:HYPOTHETICAL 30.2KD PROTEIN IN IDH-DEOR INTERGENIC REGION] [SP:P54947] 141 SPX2471 24715132 74 222 NO-HIT 6 SPX2472 2472 5133 224 672 90 2.30E-09 [LN:E69787][AC:E69787] [PN:hypothetical protein ydiL] [GN:ydiL] [OR:Bacillussubtilis] 87 SPX2473 2473 5134 303 909 229 5.80E-46 [LN:T44638][AC:T44638] [PN:capsular polysaccharide biosynthesis protein cpsY[imported]] [GN:cpsY] [CL:probable transcription regulator lsyR][OR:Streptococcus agalactiae] 172 SPX2474 2474 5135 154 462 197 1.80E-31[LN:LSPA_BACSU] [AC:Q45479] [GN:LSPA:LSP] [OR:Bacillus subtilis][EC:3.4.23.36] [DE:PEPTIDASE) (SIGNAL PEPTIDASE II) (SPASE II)][SP:Q45479] 140 SPX2475 2475 5136 296 888 888 1.80E-117 [LN:YLYB_BACSU][AC:Q45480:O31732] [GN:YLYB] [OR:Bacillus subtilis] [DE:HYPOTHETICAL33.7 KD PROTEIN IN LSP-PYRR INTERGENIC REGION (ORF-X)][SP:Q45480:O31732] 158 SPX2476 2476 5137 628 1884 461 1.70E-56[GI:1914872] [LN:SPZ82001] [AC:Z82001] [PN:PCPA] [GN:pcpA][OR:Streptococcus pneumoniae] 88 SPX2477 2477 5138 377 1131 13874.40E-185 [LN:F81125] [AC:F81125] [PN:glutamate 5-kinase NMB1069[imported]] [GN:NMB1069] [OR:Neisseria meningitidis] 107 SPX2478 24785139 421 1263 1530 1.10E-204 [GI:7413448] [LN:AE002457][AC:AE002457:AE002098] [PN:gamma-glutamyl phosphate reductase][GN:NMB1068] [OR:Neisseria meningitidis] 130 SPX2479 2479 5140 266 798396 3.30E-67 [LN:PROC_ARATH] [AC:P54904] [GN:PROC1] [OR:Arabidopsisthaliana] [SR:,Mouse-ear cress] [EC:1.5.1.2] [DE:PYRROLINE-5-CARBOXYLATEREDUCTASE, (P5CR) (P5C REDUCTASE)] [SP:P54904] 176 SPX2480 2480 5141 213639 528 4.30E-68 [LN:KTHY_BACSU] [AC:P37537] [GN:TMK] [OR:Bacillussubtilis] [EC:2.7.4.9] [DE:THYMIDYLATE KINASE, (DTMP KINASE)][SP:P37537] 125 SPX2481 2481 5142 84 252 NO-HIT 6 SPX2482 2482 5143 297891 244 4.80E-37 [LN:HOLB_BACSU] [AC:P37540] [GN:HOLB] [OR:Bacillussubtilis] [EC:2.7.7.7] [DE:DNA POLYMERASE III, DELTA′SUBUNIT,][SP:P37540] 128 SPX2483 2483 5144 106 318 103 9.60E-09 [LN:YABA_BACSU][AC:P37542] [GN:YABA] [OR:Bacillus subtilis] [DE:HYPOTHETICAL 14.1 KDPROTEIN IN XPAC-ABRB INTERGENIC REGION] [SP:P37542] 137 SPX2484 24845145 290 870 618 1.60E-84 [LN:YABC_BACSU] [AC:P37544] [GN:YABC][OR:Bacillus subtilis] [DE:HYPOTHETICAL 33.0 KD PROTEIN IN XPAC-ABRBINTERGENIC REGION] [SP:P37544] 137 SPX2485 2485 5146 182 546 3622.50E-61 [LN:S62019] [AC:S62019] [PN:hypothetical proteinYDR540c:hypothetical protein D3703.8] [GN:YDR540c] [CL:Saccharomyceshypothetical protein YDR540c] [OR:Saccharomyces cerevisiae] 177 SPX24862486 5147 168 504 82 2.90E-09 [GI:6690333] [LN:AF117259] [AC:AF117259][PN:replication protein] [GN:repX] [OR:Staphylococcus aureus] 102SPX2487 2487 5148 150 450 400 5.20E-51 [LN:S52544] [AC:S52544] [PN:ISL2protein] [OR:Lactobacillus helveticus] 71 SPX2488 2488 5149 134 402 3701.00E-54 [LN:S52544] [AC:S52544] [PN:ISL2 protein] [OR:Lactobacillushelveticus] 71 SPX2489 2489 5150 91 273 NO-HIT 6 SPX2490 2490 5151 4451335 585 1.40E-196 [LN:GID_BACSU] [AC:P39815] [GN:GID] [OR:Bacillussubtilis] [DE:GID PROTEIN] [SP:P39815] 87 SPX2491 2491 5152 246 738 7932.20E-104 [LN:F69708] [AC:F69708] [PN:uridylate kinase smbA] [GN:smbA][CL:uridine 5′-monophosphate kinase] [OR:Bacillus subtilis] 120 SPX24922492 5153 146 438 NO-HIT 6 SPX2493 2493 5154 186 558 545 2.50E-69[LN:G69626] [AC:G69626] [PN:ribosome recycling factor frr] [GN:frr][CL:ribosome releasing factor] [OR:Bacillus subtilis] 121 SPX2494 24945155 139 417 NO-HIT 6 SPX2495 2495 5156 285 855 180 3.70E-45[GI:2145404] [LN:BSY09476] [AC:Y09476] [PN:YitL] [OR:Bacillus subtilis]71 SPX2496 2496 5157 72 216 134 1.00E-13 [LN:A69931] [AC:A69931][PN:hypothetical protein yozE] [GN:yozE] [OR:Bacillus subtilis] 87SPX2497 2497 5158 323 969 956 1.30E-128 [LN:PHOL_BACSU] [AC:P46343][GN:PHOH] [OR:Bacillus subtilis] [DE:PHOH-LIKE PROTEIN] [SP:P46343] 95SPX2498 2498 5159 65 195 NO-HIT 6 SPX2499 2499 5160 167 501 87 0.00031[LN:E75272] [AC:E75272] [PN:hypothetical protein] [GN:DR2441][OR:Deinococcus radiodurans] 90 SPX2500 2500 5161 92 276 253 1.30E-28[LN:DHA_BACSU] [AC:Q08352] [GN:ALD:SPOVN] [OR:Bacillus subtilis][EC:1.4.1.1] [DE:ALANINE DEHYDROGENASE, (STAGE V SPORULATION PROTEIN N)][SP:Q08352] 151 SPX2501 2501 5162 65 195 168 5.10E-17 [LN:JE0388][AC:JE0388] [PN:alanine dehydrogenase,] [CL:alaninedehydrogenase:alanine dehydrogenase homology] [OR:Enterobacteraerogenes] [EC:1.4.1.1] 152 SPX2502 2502 5163 73 219 239 3.30E-27[LN:S74638] [AC:S74638] [PN:alanine dehydrogenase:hypothetical proteinsll1682:hypothetical protein sll1682] [CL:alanine dehydrogenase:alaninedehydrogenase homology] [OR:Synechocystis sp.] [SR:PCC 6803, , PCC 6803][SR:PCC 6803, ] 233 SPX2503 2503 5164 142 426 405 2.90E-56[LN:DHA_BACSU] [AC:Q08352] [GN:ALD:SPOVN] [OR:Bacillus subtilis][EC:1.4.1.1] [DE:ALANINE DEHYDROGENASE, (STAGE V SPORULATION PROTEIN N)][SP:Q08352] 151 SPX2504 2504 5165 196 588 147 8.00E-20 [LN:C69895][AC:C69895] [PN:conserved hypothetical protein yoaA] [GN:yoaA][CL:Escherichia coli ribosomal-protein-alanine N-acetyltransferase rimJ][OR:Bacillus subtilis] 170 SPX2505 2505 5166 217 651 1062 6.40E-138[GI:3211753] [LN:AF052208] [AC:AF052208] [PN:competence protein][GN:celA] [OR:Streptococcus pneumoniae] 104 SPX2506 2506 5167 459 13772213 0 [GI:3211754] [LN:AF052208] [AC:AF052208] [PN:competence protein][GN:celB] [OR:Streptococcus pneumoniae] 104 SPX2507 2507 5168 306 9181215 1.90E-162 [GI:3211754] [LN:AF052208] [AC:AF052208] [PN:competenceprotein] [GN:celB] [OR:Streptococcus pneumoniae] 104 SPX2508 2508 5169196 588 164 1.60E-26 [LN:YYBJ_BACSU] [AC:P37494] [GN:YYBJ] [OR:Bacillussubtilis] [DE:INTERGENIC REGION] [SP:P37494] 95 SPX2509 2509 5170 3921176 NO-HIT 6 SPX2510 2510 5171 88 264 NO-HIT 6 SPX2511 2511 5172 196588 589 4.10E-77 [LN:IF3_LISMO] [AC:O53084] [GN:INFC] [OR:Listeriamonocytogenes] [DE:TRANSLATION INITIATION FACTOR IF-3] [SP:O53084] 116SPX2512 2512 5173 67 201 235 1.10E-28 [LN:R5BS35] [AC:S05347][PN:ribosomal protein L35] [GN:rpmI] [CL:Escherichia coli ribosomalprotein L35] [OR:Bacillus stearothermophilus] 137 SPX2513 2513 5174 120360 476 9.30E-63 [LN:RL20_BACSU] [AC:P55873] [GN:RPLT] [OR:Bacillussubtilis] [DE:50S RIBOSOMAL PROTEIN L20] [SP:P55873] 103 SPX2514 25145175 127 381 130 6.20E-24 [LN:LGUL_HAEIN] [AC:P44638] [GN:GLOA:HI0323][OR:Haemophilus influenzae] [EC:4.4.1.5] [DE:(S-D-LACTOYLGLUTATHIONEMETHYLGLYOXAL LYASE)] [SP:P44638] 147 SPX2515 2515 5176 190 570 3542.10E-55 [LN:YLXD_BACCL] [AC:P46536] [OR:Bacillus caldolyticus][DE:HYPOTHETICAL 27.6 KD PROTEIN IN PYRAB-PYRD INTERGENIC REGION (ORF2)][SP:P46536] 139 SPX2516 2516 5177 94 282 172 7.70E-23 [LN:YLXD_BACCL][AC:P46536] [OR:Bacillus caldolyticus] [DE:HYPOTHETICAL 27.6 KD PROTEININ PYRAB-PYRD INTERGENIC REGION (ORF2)] [SP:P46536] 139 SPX2517 25175178 313 939 563 8.20E-147 [LN:PYDB_LACLC] [AC:P54322] [GN:PYRDB][OR:Lactococcus lactis] [SR:,subspcremoris:Streptococcus cremoris][EC:1.3.3.1] [DE:(DHODEHASE B) (DHODB)] [SP:P54322] 159 SPX2518 25185179 722 2166 2390 0 [GI:4218533] [LN:SPN010312] [AC:AJ010312][PN:endo-beta-N-acetylglucosaminidase] [GN:lytB] [FN:cell walldegradation and cell separation] [OR:Streptococcus pneumoniae] 167SPX2519 2519 5180 561 1683 2767 0 [GI:6175915] [LN:AF181976][AC:AF181976] [PN:adherence and virulence protein A] [GN:pavA][FN:adhesin] [OR:Streptococcus pneumoniae] 132 SPX2520 2520 5181 77 231NO-HIT 6 SPX2521 2521 5182 166 498 705 5.20E-92 [GI:2749950][LN:AF000954] [AC:AF000954] [OR:Streptococcus mutans] 66 SPX2522 25225183 132 396 507 6.90E-71 [LN:A36933] [AC:A36933] [PN:diacylglycerolkinase homolog] [CL:Bacillus subtilis diacylglycerol kinase dgkA][OR:Streptococcus mutans] 134 SPX2523 2523 5184 300 900 1502 1.40E-204[GI:5305399] [LN:AF072811] [AC:AF072811] [PN:GTPase Era] [GN:era][OR:Streptococcus pneumoniae] 95 SPX2524 2524 5185 275 825 892 1.90E-119[LN:FPG_STRMU] [AC:P55045] [GN:MUTM:FPG] [OR:Streptococcus mutans][EC:3.2.2.23] [DE:GLYCOSYLASE)] [SP:P55045] 110 SPX2525 2525 5186 61 183NO-HIT 6 SPX2526 2526 5187 203 609 167 2.40E-32 [LN:Y553_SYNY3][AC:Q55515] [GN:SLR0553] [OR:Synechocystis sp] [SR:,strain PCC 6803][DE:HYPOTHETICAL 22.5 KD PROTEIN SLR0553] [SP:Q55515] 140 SPX2527 25275188 67 201 NO-HIT 6 SPX2528 2528 5189 400 1200 1989 9.60E-280[GI:3820455] [LN:SPN7367] [AC:AJ007367] [PN:multi-drug resistance effluxpump] [GN:pmrA] [OR:Streptococcus pneumoniae] 118 SPX2529 2529 5190 50150 177 8.70E-20 [LN:RL33_LACLA] [AC:P27167] [GN:RPMG] [OR:Lactococcuslactis] [SR:,subsplactis:Streptococcus lactis] [DE:50S RIBOSOMAL PROTEINL33] [SP:P27167] 145 SPX2530 2530 5191 78 234 82 8.20E-06 [LN:A70028][AC:A70028] [PN:hypothetical protein yvaL] [GN:yvaL] [CL:protein-exportprotein secG] [OR:Bacillus subtilis] 120 SPX2531 2531 5192 785 2355 5644.00E-180 [LN:G70027] [AC:G70027] [PN:conserved hypothetical proteinyvaJ] [GN:yvaJ] [CL:virulence-associated protein vacB homolog][OR:Bacillus subtilis] 144 SPX2532 2532 5193 156 468 793 1.30E-104[GI:3211758] [LN:AF052209] [AC:AF052209] [PN:VacB homolog][OR:Streptococcus pneumoniae] 88 SPX2533 2533 5194 287 861 14998.30E-203 [GI:4883699] [LN:AF079807] [AC:AF079807] [PN:telluriteresistance protein TehB] [GN:tehB] [OR:Streptococcus pneumoniae] 119SPX2534 2534 5195 129 387 326 5.30E-41 [GI:3211758] [LN:AF052209][AC:AF052209] [PN:VacB homolog] [OR:Streptococcus pneumoniae] 88 SPX25352535 5196 74 222 NO-HIT 6 SPX2536 2536 5197 318 954 800 5.10E-182[GI:3211759] [LN:AF052209] [AC:AF052209] [PN:competence protein][GN:coiA] [OR:Streptococcus pneumoniae] 104 SPX2537 2537 5198 601 18032159 2.10E-292 [LN:PEPB_STRAG] [AC:Q53778] [GN:PEPB] [OR:Streptococcusagalactiae] [EC:3.4.24.-] [DE:GROUP B OLIGOPEPTIDASE PEPB,] [SP:Q53778]129 SPX2538 2538 5199 238 714 680 4.90E-90 [GI:1771204] [LN:LLLVSFPEP][AC:X99710] [PN:methyltransferase] [OR:Lactococcus lactis] 86 SPX25392539 5200 314 942 189 3.10E-32 [LN:PRTM_LACPA] [AC:Q02473] [GN:PRTM][OR:Lactobacillus paracasei] [DE:PROTEASE MATURATION PROTEIN PRECURSOR][SP:Q02473] 121 SPX2540 2540 5201 114 342 567 4.00E-74 [GI:1490399][LN:SPPARCETP] [AC:Z67739] [PN:DNA transposase] [OR:Streptococcuspneumoniae] 90 SPX2541 2541 5202 191 573 422 2.30E-53 [LN:B30868][AC:B30868] [PN:hypothetical protein 1] [OR:Streptococcus agalactiae] 81SPX2542 2542 5203 91 273 NO-HIT 6 SPX2543 2543 5204 64 192 NO-HIT 6SPX2544 2544 5205 207 621 86 4.90E-12 [LN:T46083] [AC:T46083][PN:hypothetical protein T20E23.120] [CL:Aquifex aeolicusphosphoglycerate mutase:phosphoglycerate mutase homology][OR:Arabidopsis thaliana] [SR:, mouse-ear cress] 190 SPX2545 2545 5206161 483 210 1.70E-35 [LN:EBSC_ENTFA] [AC:P36922] [OR:Enterococcusfaecalis] [SR:,Streptococcus faecalis] [DE:EBSC PROTEIN] [SP:P36922] 115SPX2546 2546 5207 281 843 128 6.60E-17 [LN:B72411] [AC:B72411][PN:conserved hypothetical protein] [GN:TM0164] [OR:Thermotoga maritima]96 SPX2547 2547 5208 263 789 102 2.10E-09 [GI:1865711] [LN:BPPLYBA][AC:Y11477] [PN:endolysin] [GN:plyBa] [FN:cell wall hydrolase][OR:Bacteriophage Bastille] 116 SPX2548 2548 5209 460 1380 11801.90E-156 [LN:S66080] [AC:S66080:I40018:C69629:S05371:S18903][PN:UDP-N-acetylglucosamine pyrophosphorylase gcaD:cell division proteintms26:tms protein] [GN:gcaD:tms26] [CL:N-acetylglucosamine-1-phosphateuridyltransferase] [OR:Bacillus subtilis] 237 SPX2549 2549 5210 182 546167 2.40E-45 [LN:YQKG_BACSU] [AC:P54570] [GN:YQKG] [OR:Bacillussubtilis] [DE:HYPOTHETICAL 21.0 KD PROTEIN IN GLNQ-ANSR INTERGENICREGION] [SP:P54570] 137 SPX2550 2550 5211 105 315 NO-HIT 6 SPX2551 25515212 231 693 477 1.60E-61 [LN:PFS_ECOLI] [AC:P24247] [GN:PFS][OR:Escherichia coli] [EC:3.2.2.16:3.2.2.9] [DE:(EC 3.2.2.9)]][SP:P24247] 110 SPX2552 2552 5213 164 492 124 1.90E-12 [GI:2769573][LN:LLCPJW565] [AC:Y12736] [OR:Lactococcus lactis subsp. cremoris] 79SPX2553 2553 5214 197 591 137 1.00E-08 [LN:DPO3_BACSU] [AC:P13267][GN:POLC:DNAF:MUTI] [OR:Bacillus subtilis] [EC:2.7.7.7] [DE:DNAPOLYMERASE III, ALPHA CHAIN POLC-TYPE, (POLIII)] [SP:P13267] 154 SPX25542554 5215 257 771 105 1.40E-11 [LN:E69827] [AC:E69827][PN:glycerophosphodiester phosphodiesterase homolog yhdW] [GN:yhdW][CL:glycerophosphodiester phosphodiesterase] [OR:Bacillus subtilis] 159SPX2555 2555 5216 116 348 577 5.80E-76 [GI:4200438] [LN:AF026471][AC:AF026471] [PN:putative transposase] [OR:Streptococcus pneumoniae] 96SPX2556 2556 5217 47 141 186 5.40E-22 [GI:5019553] [LN:SPN239004][AC:AJ239004] [PN:putative transposase] [OR:Streptococcus pneumoniae] 97SPX2557 2557 5218 67 201 NO-HIT 6 SPX2558 2558 5219 211 633 NO-HIT 6SPX2559 2559 5220 100 300 84 0.00082 [GI:1707287] [LN:BBU80959][AC:U80959:L78251] [PN:putative outer membrane protein] [GN:ospFi][OR:Borrelia burgdorferi] [SR:Lyme disease spirochete] 148 SPX2560 25605221 236 708 267 1.40E-53 [LN:YE54_HAEIN] [AC:P44202] [GN:HI1454][OR:Haemophilus influenzae] [DE:HYPOTHETICAL CYTOCHROME C-TYPEBIOGENESIS PROTEIN HI1454] [SP:P44202] 141 SPX2561 2561 5222 186 558 2396.40E-28 [LN:YE53_HAEIN] [AC:Q57127:O05062] [GN:HI1453] [OR:Haemophilusinfluenzae] [DE:HYPOTHETICAL PROTEIN HI1453 PRECURSOR][SP:Q57127:O05062] 136 SPX2562 2562 5223 464 1392 481 1.60E-122[LN:D69814] [AC:D69814] [PN:metabolite transporter homolog yfnA][GN:yfnA] [CL:arginine permease] [OR:Bacillus subtilis] 120 SPX2563 25635224 308 924 985 7.10E-129 [LN:T46757] [AC:T46757] [PN:lipoprotein lmb[validated]] [GN:lmb] [OR:Streptococcus agalactiae] 95 SPX2564 2564 5225839 2517 409 3.50E-104 [LN:T46758] [AC:T46758] [PN:hypothetical protein[imported]] [OR:Streptococcus agalactiae] 90 SPX2565 2565 5226 1040 3120400 1.50E-93 [LN:T46758] [AC:T46758] [PN:hypothetical protein[imported]] [OR:Streptococcus agalactiae] 90 SPX2566 2566 5227 63 189NO-HIT 6 SPX2567 2567 5228 63 189 240 1.40E-26 [LN:T46758] [AC:T46758][PN:hypothetical protein [imported]] [OR:Streptococcus agalactiae] 90SPX2568 2568 5229 67 201 104 3.80E-14 [LN:T46758] [AC:T46758][PN:hypothetical protein [imported]] [OR:Streptococcus agalactiae] 90SPX2569 2569 5230 161 483 152 4.70E-20 [LN:T46758] [AC:T46758][PN:hypothetical protein [imported]] [OR:Streptococcus agalactiae] 90SPX2570 2570 5231 80 240 NO-HIT 6 SPX2571 2571 5232 86 258 NO-HIT 6SPX2572 2572 5233 145 435 107 6.20E-05 [GI:7228476] [LN:AF163151][AC:AF163151] [PN:dentin sialophosphoprotein precursor] [GN:DSPP][OR:Homo sapiens] [SR:human] 121 SPX2573 2573 5234 408 1224 9617.20E-190 [LN:PEPT_LACLC] [AC:P42020] [GN:PEPT] [OR:Lactococcus lactis][SR:,subspcremoris:Streptococcus cremoris] [EC:3.4.11.-] [DE:PEPTIDASET, (AMINOTRIPEPTIDASE) (TRIPEPTIDASE)] [SP:P42020] 185 SPX2574 2574 5235365 1095 215 4.70E-41 [LN:HEMZ_BACSU] [AC:P32396] [GN:HEMH:HEMF][OR:Bacillus subtilis] [EC:4.99.1.1] [DE:SYNTHETASE)] [SP:P32396] 108SPX2575 2575 5236 126 378 149 2.80E-25 [GI:6136300] [LN:AF065159][AC:AF065159] [PN:MscL] [GN:mscL] [OR:Bradyrhizobium japonicum] 90SPX2576 2576 5237 87 261 NO-HIT 6 SPX2577 2577 5238 129 387 180 3.60E-29[LN:T44787] [AC:T44787] [PN:glucokinase, [imported]] [CL:glucosekinase:glucose kinase homology] [OR:Bacillus megaterium] [EC:2.7.1.2]136 SPX2578 2578 5239 88 264 61 0.0009 [GI:2897104] [LN:AF020798][AC:AF020798] [PN:putative host cell surface-exposed lipoprotein][OR:Streptococcus thermophilus bacteriophage TP-J34] 145 SPX2579 25795240 273 819 279 1.60E-30 [GI:4218526] [LN:SPAJ9639] [AC:AJ009639][PN:1,4-beta-N-acetylmuramidase] [GN:lytC] [FN:lysis of cell wallpeptidoglycan] [OR:Streptococcus pneumoniae] 153 SPX2580 2580 5241 5101530 289 6.20E-30 [GI:4218526] [LN:SPAJ9639] [AC:AJ009639][PN:1,4-beta-N-acetylmuramidase] [GN:lytC] [FN:lysis of cell wallpeptidoglycan] [OR:Streptococcus pneumoniae] 153 SPX2581 2581 5242 5741722 339 6.40E-76 [LN:A71951] [AC:A71951] [PN:p-aminobenzoatesynthetase] [GN:pabB] [OR:Helicobacter pylori] [SR:strain J99, , strainJ99] [SR:strain J99, ] 140 SPX2582 2582 5243 1964 5892 7027 0[GI:6911257] [LN:AF221126] [AC:AF221126] [PN:putative zincmetalloprotease] [GN:zmpB] [OR:Streptococcus pneumoniae] 115 SPX25832583 5244 78 234 NO-HIT 6 SPX2584 2584 5245 108 324 71 7.10E-06[GI:501027] [LN:TBU01849] [AC:U01849] [OR:Kinetoplast Trypanosomabrucei] [SR:Trypanosoma brucei] 97 SPX2585 2585 5246 188 564 3921.60E-49 [LN:YWLG_BACSU] [AC:P39157] [GN:YWLG:IPC-33D] [OR:Bacillussubtilis] [DE:HYPOTHETICAL 19.4 KD PROTEIN IN SPOIIR-GLYC INTERGENICREGION] [SP:P39157] 147 SPX2586 2586 5247 378 1134 1862 7.80E-253[GI:6911256] [LN:AF221126] [AC:AF221126] [PN:putative histidine kinase][GN:zmpS] [OR:Streptococcus pneumoniae] 111 SPX2587 2587 5248 63 189NO-HIT 6 SPX2588 2588 5249 186 558 898 5.90E-119 [GI:6911256][LN:AF221126] [AC:AF221126] [PN:putative histidine kinase] [GN:zmpS][OR:Streptococcus pneumoniae] 111 SPX2589 2589 5250 246 738 12372.00E-167 [GI:6911255] [LN:AF221126] [AC:AF221126] [PN:putative responseregulator] [GN:zmpR] [OR:Streptococcus pneumoniae] 113 SPX2590 2590 5251371 1113 1110 1.40E-147 [LN:YE55_HAEIN] [AC:P45213] [GN:HI1455][OR:Haemophilus influenzae] [DE:HYPOTHETICAL PROTEIN HI1455] [SP:P45213]112 SPX2591 2591 5252 198 594 335 9.20E-41 [LN:YE53_HAEIN][AC:Q57127:O05062] [GN:HI1453] [OR:Haemophilus influenzae][DE:HYPOTHETICAL PROTEIN HI1453 PRECURSOR] [SP:Q57127:O05062] 136SPX2592 2592 5253 237 711 139 3.50E-49 [LN:YE54_HAEIN] [AC:P44202][GN:HI1454] [OR:Haemophilus influenzae] [DE:HYPOTHETICAL CYTOCHROMEC-TYPE BIOGENESIS PROTEIN HI1454] [SP:P44202] 141 SPX2593 2593 5254 287861 312 4.30E-47 [GI:3608389] [LN:AF071085] [AC:AF071085] [PN:Orfde2][OR:Enterococcus faecalis] 79 SPX2594 2594 5255 685 2055 564 1.00E-82[LN:E70040] [AC:E70040] [PN:conserved hypothetical protein yvgP][GN:yvgP] [CL:hypothetical protein yvgP] [OR:Bacillus subtilis] 128SPX2595 2595 5256 64 192 NO-HIT 6 SPX2596 2596 5257 85 255 NO-HIT 6SPX2597 2597 5258 63 189 NO-HIT 6 SPX2598 2598 5259 188 564 221 1.00E-42[LN:E69999] [AC:E69999] [PN:hypothetical protein ytqB] [GN:ytqB][OR:Bacillus subtilis] 87 SPX2599 2599 5260 149 447 329 6.50E-47[LN:D69999] [AC:D69999] [PN:conserved hypothetical protein ytqA][GN:ytqA] [CL:Methanococcus jannaschii conserved hypothetical proteinMJ0486] [OR:Bacillus subtilis] 165 SPX2600 2600 5261 84 252 209 2.10E-24[LN:D69999] [AC:D69999] [PN:conserved hypothetical protein ytqA][GN:ytqA] [CL:Methanococcus jannaschii conserved hypothetical proteinMJ0486] [OR:Bacillus subtilis] 165 SPX2601 2601 5262 146 438 2102.60E-23 [LN:D69999] [AC:D69999] [PN:conserved hypothetical proteinytqA] [GN:ytqA] [CL:Methanococcus jannaschii conserved hypotheticalprotein MJ0486] [OR:Bacillus subtilis] 165 SPX2602 2602 5263 120 360NO-HIT 6 SPX2603 2603 5264 82 246 182 1.20E-19 [GI:1022726][LN:SHU35635] [AC:U35635] [PN:unknown] [OR:Staphylococcus haemolyticus][SR:Staphylococcus haemolyticus strain=Y176] 129 SPX2604 2604 5265 208624 156 1.10E-37 [GI:6332767] [LN:AB033763][AC:AB033763:AB014419:AB014429:AB014439] [PN:hypothetical protein][OR:Staphylococcus aureus] [SR:Staphylococcus aureus (strain:NCTC10442)DNA, clone_lib:Lambda das] 194 SPX2605 2605 5266 2173 6519 309 2.70E-130[GI:6468240] [LN:SCF81] [AC:AL133171] [PN:putative secretedbeta-galactosidase] [GN:SCF81.25c] [OR:Streptomyces coelicolor A3(2)]129 SPX2606 2606 5267 62 186 NO-HIT 6 SPX2607 2607 5268 64 192 NO-HIT 6SPX2608 2608 5269 144 432 184 6.10E-21 [LN:T30285] [AC:T30285][PN:hypothetical protein] [OR:Streptococcus pneumoniae] 79 SPX2609 26095270 262 786 92 2.70E-11 [LN:SGCC_ECOLI] [AC:P39365] [GN:SGCC][OR:Escherichia coli] [DE:PUTATIVE PHOSPHOTRANSFERASE ENZYME II, CCOMPONENT SGCC] [SP:P39365] 134 SPX2610 2610 5271 231 693 231 3.70E-25[GI:1736815] [LN:D90848] [AC:D90848:AB001340] [PN:PTS system,Galactitol-specific IIC component] [GN:gatC] [OR:Escherichia coli][SR:Escherichia coli (strain:K12) DNA, clone_lib:Kohara lambda minise]201 SPX2611 2611 5272 102 306 NO-HIT 6 SPX2612 2612 5273 159 477 955.10E-13 [GI:4512375] [LN:AB011837] [AC:AB011837] [PN:phosphotransferasesystem (PTS)] [GN:fruA] [OR:Bacillus halodurans] [SR:Bacillus halodurans(strain:C-125) DNA, clone_lib:lambda no.9] 181 SPX2613 2613 5274 21396417 10556 0 [GI:5726291] [LN:AF127143] [AC:AF127143] [PN:cellwall-associated serine proteinase precursor] [GN:prtA] [OR:Streptococcuspneumoniae] 134 SPX2614 2614 5275 68 204 136 2.70E-14 [LN:T30285][AC:T30285] [PN:hypothetical protein] [OR:Streptococcus pneumoniae] 79SPX2615 2615 5276 66 198 NO-HIT 6 SPX2616 2616 5277 262 786 107 2.30E-18[GI:7635999] [LN:SCE6] [AC:AL353832] [PN:putative integral membranetransport protein.] [GN:SCE6.32c] [OR:Streptomyces coelicolor A3(2)] 136SPX2617 2617 5278 287 861 113 2.80E-10 [GI:7636000] [LN:SCE6][AC:AL353832] [PN:putative integral membrane protein.] [GN:SCE6.33c][OR:Streptomyces coelicolor A3(2)] 126 SPX2618 2618 5279 318 954 6011.60E-83 [LN:G75548] [AC:G75548] [PN:ABC transporter, ATP-bindingprotein] [GN:DR0205] [CL:unassigned ATP-binding cassetteproteins:ATP-binding cassette homology] [OR:Deinococcus radiodurans] 184SPX2619 2619 5280 83 249 NO-HIT 6 SPX2620 2620 5281 132 396 NO-HIT 6SPX2621 2621 5282 158 474 123 3.70E-11 [GI:1914870] [LN:SPZ82001][AC:Z82001] [PN:unknown] [OR:Streptococcus pneumoniae] 81 SPX2622 26225283 230 690 765 9.20E-100 [LN:RL1_BACST] [AC:P04447] [GN:RPLA][OR:Bacillus stearothermophilus] [DE:50S RIBOSOMAL PROTEIN L1][SP:P04447] 111 SPX2623 2623 5284 142 426 596 4.50E-77 [LN:S38871][AC:S38871] [PN:ribosomal protein L11] [GN:rplK] [CL:Escherichia coliribosomal protein L11] [OR:Staphylococcus carnosus] 133 SPX2624 26245285 75 225 NO-HIT 6 SPX2625 2625 5286 239 717 133 3.00E-20 [GI:2529473][LN:AF006665] [AC:AF006665] [PN:YokZ] [GN:yokZ] [FN:unknown][OR:Bacillus subtilis] 96 SPX2626 2626 5287 60 180 NO-HIT 6 SPX2627 26275288 170 510 103 7.80E-07 [LN:A81062] [AC:A81062] [PN:conservedhypothetical protein NMB1619 [imported]] [GN:NMB1619] [OR:Neisseriameningitidis] 119 SPX2628 2628 5289 72 216 187 1.80E-19 [LN:B71121][AC:B71121] [PN:hypothetical protein PH0737] [GN:PH0737][CL:thermophilic aminopeptidase I alpha chain] [OR:Pyrococcushorikoshii] 142 SPX2629 2629 5290 199 597 306 4.10E-72 [LN:C69830][AC:C69830] [PN:glucanase homolog yhfE] [GN:yhfE] [CL:thermophilicaminopeptidase I alpha chain] [OR:Bacillus subtilis] 131 SPX2630 26305291 114 342 145 6.70E-14 [GI:2315995] [LN:SAU87144] [AC:U87144][PN:branched-chain amino acid carrier protein] [OR:Staphylococcusaureus] 112 SPX2631 2631 5292 447 1341 391 6.60E-90 [LN:BRNQ_BACSU][AC:P94499:O07082] [GN:BRNQ] [OR:Bacillus subtilis] [DE:CHAIN AMINO ACIDUPTAKE CARRIER)] [SP:P94499:O07082] 124 SPX2632 2632 5293 63 189 883.10E-06 [LN:YC61_SYNY3] [AC:P73801] [GN:SLR1261] [OR:Synechocystis sp][SR:,strain PCC 6803] [DE:HYPOTHETICAL 19.1 KD PROTEIN SLR1261][SP:P73801] 140 SPX2633 2633 5294 80 240 100 1.90E-17 [GI:1914870][LN:SPZ82001] [AC:Z82001] [PN:unknown] [OR:Streptococcus pneumoniae] 81SPX2634 2634 5295 193 579 548 7.70E-95 [GI:3212185] [LN:U32707][AC:U32707:L42023] [PN:H. influenzae predicted coding region HI0220.2][GN:HI0220.2] [OR:Haemophilus influenzae Rd] 140 SPX2635 2635 5296 4671401 646 4.20E-200 [GI:2160707] [LN:LLU78036] [AC:U78036][PN:dipeptidase] [OR:Lactococcus lactis] 79 SPX2636 2636 5297 202 606113 2.60E-17 [LN:NOX_THETH] [AC:Q60049:Q53306] [GN:NOX] [OR:Thermusaquaticus] [SR:,subspthermophilus] [EC:1.6.99.3] [DE:(NADH:OXYGENOXIDOREDUCTASE)] [SP:Q60049:Q53306] 158 SPX2637 2637 5298 80 240 NO-HIT6 SPX2638 2638 5299 267 801 141 2.90E-22 [GI:2108229] [LN:LFU97348][AC:U97348] [PN:basic surface protein] [FN:L-cystine transporter][OR:Lactobacillus fermentum] 121 SPX2639 2639 5300 278 834 106 6.20E-12[LN:G75297] [AC:G75297] [PN:conserved hypothetical protein] [GN:DR2233][CL:probable phosphoesterase MJ0912:phosphoesterase core homology][OR:Deinococcus radiodurans] 167 SPX2640 2640 5301 615 1845 18825.00E-256 [LN:UVRC_BACSU] [AC:P14951] [GN:UVRC] [OR:Bacillus subtilis][DE:EXCINUCLEASE ABC SUBUNIT C] [SP:P14951] 104 SPX2641 2641 5302 241723 NO-HIT 6 SPX2642 2642 5303 411 1233 95 3.90E-07 [LN:SPN250764][AC:AJ250764] [PN:MurM protein] [GN:murM] [FN:serine/alanine addingenzyme] [OR:Streptococcus pneumoniae] 120 SPX2643 2643 5304 407 12212088 3.50E-283 [LN:SPN277484] [AC:AJ277484] [PN:beta-lactam resistancefactor] [GN:fibA] [FN:putative role in peptidoglycan crosslinking][OR:Streptococcus pneumoniae] 152 SPX2644 2644 5305 260 780 4827.10E-100 [GI:7453516] [LN:AF157484] [AC:AF157484] [PN:tributyrinesterase] [GN:estA] [OR:Lactococcus lactis subsp. lactis] 113 SPX26452645 5306 554 1662 581 1.80E-136 [LN:H69884] [AC:H69884] [PN:conservedhypothetical protein ymfA] [GN:ymfA] [CL:conserved hypothetical proteinMG139] [OR:Bacillus subtilis] 139 SPX2646 2646 5307 647 1941 5293.20E-120 [LN:H69980] [AC:H69980] [PN:single-strand DNA-specificexonuclease homolog yrvE] [GN:yrvE] [OR:Bacillus subtilis] 113 SPX26472647 5308 741 2223 529 8.40E-150 [LN:H69980] [AC:H69980][PN:single-strand DNA-specific exonuclease homolog yrvE] [GN:yrvE][OR:Bacillus subtilis] 113 SPX2648 2648 5309 253 759 527 8.90E-103[LN:GLNQ_BACST] [AC:P27675] [GN:GLNQ] [OR:Bacillus stearothermophilus][DE:GLUTAMINE TRANSPORT ATP-BINDING PROTEIN GLNQ] [SP:P27675] 132SPX2649 2649 5310 65 195 69 0.00063 [LN:E72756] [AC:E72756][PN:hypothetical protein APE0042] [GN:APE0042] [OR:Aeropyrum pernix] 92SPX2650 2650 5311 73 219 92 9.10E-12 [LN:G72510] [AC:G72510][PN:hypothetical protein APE2061] [GN:APE2061] [OR:Aeropyrum pernix] 92SPX2651 2651 5312 265 795 422 2.40E-66 [LN:PEB1_CAMJE] [AC:P45678][GN:PEB1A] [OR:Campylobacter jejuni] [DE:MAJOR CELL-BINDING FACTORPRECURSOR (CBF1) (PEB1)] [SP:P45678] 131 SPX2652 2652 5313 226 678 4003.80E-74 [LN:G81365] [AC:G81365] [PN:probable ABC-type amino-acidtransporter permease protein Cj0920c [imported]] [GN:Cj0920c][OR:Campylobacter jejuni] 144 SPX2653 2653 5314 220 660 234 2.00E-50[LN:F69633] [AC:F69633] [PN:glutamine ABC transporter (membrane protein)glnP] [GN:glnP] [CL:histidine permease protein M] [OR:Bacillus subtilis]145 SPX2654 2654 5315 401 1203 78 7.00E-08 [GI:1255667] [LN:PSEORF1][AC:D84146] [PN:reductase] [GN:pahA] [OR:Pseudomonas aeruginosa][SR:Pseudomonas aeruginosa (strain:PaK1) DNA] 136 SPX2655 2655 5316 294882 1498 3.00E-201 [LN:ALF_STRPN] [AC:O65944] [GN:FBA] [OR:Streptococcuspneumoniae] [EC:4.1.2.13] [DE:FRUCTOSE-BISPHOSPHATE ALDOLASE,][SP:O65944] 130 SPX2656 2656 5317 443 1329 2174 1.90E-297 [GI:4583524][LN:AF140356] [AC:AF140356] [PN:VncS] [GN:vncS] [FN:putative histidinekinase/phosphatase] [OR:Streptococcus pneumoniae] 133 SPX2657 2657 5318219 657 1089 1.00E-146 [GI:4583523] [LN:AF140356] [AC:AF140356][PN:VncR] [GN:vncR] [FN:putative response regulator] [OR:Streptococcuspneumoniae] 123 SPX2658 2658 5319 460 1380 2273 0 [GI:5712669][LN:AF140784] [AC:AF140784] [PN:Vexp3] [GN:vex3] [OR:Streptococcuspneumoniae] 91 SPX2659 2659 5320 216 648 1066 2.30E-141 [GI:5712668][LN:AF140784] [AC:AF140784] [PN:Vexp2] [GN:vex2] [OR:Streptococcuspneumoniae] 91 SPX2660 2660 5321 426 1278 2070 2.40E-280 [GI:5712667][LN:AF140784] [AC:AF140784] [PN:Vexp1] [GN:vex1] [OR:Streptococcuspneumoniae] 91 SPX2661 2661 5322 85 255 NO-HIT 6

1. An isolated nucleic acid encoding a S. pneumoniae surface proteinhaving at least 98% identity to SEQ ID NO:
 4360. 2. A recombinantexpression vector comprising the nucleic acid of claim 1 operably linkedto a transcription regulatory element.
 3. A cell comprising therecombinant expression vector of claim
 2. 4. An isolated nucleic acidhaving at least 99% identity to SEQ ID NO: 1699, wherein the isolatednucleic acid encodes an S. pneumoniae surface protein.
 5. A recombinantexpression vector comprising the nucleic acid of claim 4 operably linkedto a transcription regulatory element.
 6. A cell comprising therecombinant expression vector of claim
 5. 7. An isolated nucleic acidselected from the group consisting of: a) a nucleic acid having at least99% identity to SEQ ID NO: 1699; b) a nucleic acid fully complementaryto a nucleic acid having at least 99% identity to SEQ ID NO: 1699; andc) an RNA of a) or b), wherein U is substituted for T; wherein theisolated nucleic acid encodes an S. pneumoniae surface protein.
 8. Arecombinant expression vector comprising the nucleic acid of claim 7operably linked to a transcription regulatory element.
 9. A cellcomprising the recombinant expression vector of claim
 8. 10. An isolatednucleic acid selected from the group consisting of: a) a nucleic acidencoding a S. pneumoniae surface protein having at least 98% identity toSEQ ID NO: 4360; b) a nucleic acid fully complementary to a nucleic acidencoding an S. pneumoniae surface protein having at least 98% identityto SEQ ID NO: 4360; and c) an RNA of a) or b), wherein U is substitutedfor T.
 11. A recombinant expression vector comprising the nucleic acidof claim 10 operably linked to a transcription regulatory element.
 12. Acell comprising the recombinant expression vector of claim 11.